|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
352-978 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1028.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 352 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 431
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 432 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 511
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 512 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 590
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 591 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 670
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 671 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMH 750
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 751 GGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 830
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 831 WSVGGKGSVDLARAVREAASKRSR-FQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 909
Cdd:PLN02759 489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 36796743 910 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGLF 978
Cdd:PLN02759 569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
360-978 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 985.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 360 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 439
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 440 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 519
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 520 nrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHY 599
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 600 RQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 679
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 680 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGgpsvtag 759
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 760 vPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 839
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 840 DLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQP 918
Cdd:pfam01268 417 ELAEAVVEACeEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 919 DKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTEtEQVKGLF 978
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
374-977 |
0e+00 |
|
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrofolate. FTHFS is a highly expressed key enzyme in both the Wood-Ljungdahl pathway of autotrophic CO2 fixation (acetogenesis) and the glycine synthase/reductase pathways of purinolysis. The key physiological role of this enzyme in acetogens is to catalyze the formylation of tetrahydrofolate, an initial step in the reduction of carbon dioxide and other one-carbon precursors to acetate. In purinolytic organisms, the enzymatic reaction is reversed, liberating formate from 10-formyltetrahydrofolate with concurrent production of ATP.
Pssm-ID: 349750 Cd Length: 540 Bit Score: 935.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 374 VDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 453
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 454 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvplvngvrefs 533
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 534 eiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIM 613
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 614 AVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 693
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 694 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGvplkkeytEENIQL 773
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 774 VADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAASK-R 852
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKpK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 853 SRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFILPIS 932
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 36796743 933 DVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVKGL 977
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
359-978 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 877.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 359 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 438
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 439 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 518
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 519 ynrlvplvngvrefseiqlarlkklginktdpstlteeevskfaRLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGH 598
Cdd:COG2759 153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 599 YRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 678
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 679 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvta 758
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 759 gvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 838
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 839 VDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQ 917
Cdd:COG2759 417 EELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 36796743 918 PDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVKGLF 978
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
193-335 |
8.49e-67 |
|
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NAD(P) binding domains of methylene-tetrahydrofolate dehydrogenase (m-THF DH) and m-THF DH/cyclohydrolase bifunctional enzymes (m-THF DH/cyclohydrolase). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, mono-functional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express a monofunctional DH. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133451 Cd Length: 140 Bit Score: 220.07 E-value: 8.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 193 GDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSP 272
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 36796743 273 KPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 335
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
183-338 |
2.07e-35 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 131.82 E-value: 2.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 183 TDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLH 262
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 263 EADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHF--------------GGlieeddVILLAAALRIQ 328
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGD--VDFenvkekasaitpvpGG------VGPMTVAMLLQ 150
|
170
....*....|
gi 36796743 329 NMVSSGRRWL 338
Cdd:pfam02882 151 NTVEAAKRQL 160
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
97-289 |
3.56e-33 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 129.75 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 97 KPVLAIIQAGDD--------NLmqeinQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ------ISE 162
Cdd:COG0190 32 TPGLAVVLVGDDpasqvyvrNK-----HKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 163 NlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAhgSLE-----AALq 237
Cdd:COG0190 107 E----AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVGR--SNIvgkplALL- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 36796743 238 cLFQRKGSMTM--SiqwKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 289
Cdd:COG0190 178 -LLRRNATVTVchS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
52-290 |
1.45e-25 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 109.28 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 52 PQDGQARSSCSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFK------PVLAIIQAGDDNLMQEINQN---LAEEA 122
Cdd:PLN02897 35 PENWIPYSDPPPPVSFETEQKTVVIDGNVIAEEIRTKIASEVRKMKkavgkvPGLAVVLVGQQRDSQTYVRNkikACEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 123 GLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFV 200
Cdd:PLN02897 115 GIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 201 SPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLT 280
Cdd:PLN02897 195 SCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGS 274
|
250
....*....|
gi 36796743 281 WIQPGTTVLN 290
Cdd:PLN02897 275 WLKPGAVVID 284
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
98-290 |
1.44e-24 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 104.97 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 98 PVLAIIQAG---DDNLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 172
Cdd:PLN02516 40 PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVHGILVQLPlpKHINEEKILNE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 252
Cdd:PLN02516 120 ISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHS 199
|
170 180 190
....*....|....*....|....*....|....*...
gi 36796743 253 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PLN02516 200 RTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
90-180 |
1.50e-17 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 79.37 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 90 QEKNPAFKPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENL 164
Cdd:pfam00763 20 ALKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlpLPKHI 99
|
90
....*....|....*.
gi 36796743 165 FSNKVLNALKPEKDVD 180
Cdd:pfam00763 100 DEEKVLEAIDPEKDVD 115
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
352-978 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1028.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 352 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 431
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 432 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 511
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 512 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 590
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 591 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 670
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 671 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMH 750
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 751 GGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYH 830
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 831 WSVGGKGSVDLARAVREAASKRSR-FQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 909
Cdd:PLN02759 489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 36796743 910 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGLF 978
Cdd:PLN02759 569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
360-978 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 985.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 360 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 439
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 440 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 519
Cdd:pfam01268 81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 520 nrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHY 599
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 600 RQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 679
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 680 GPFANIAHGNSSVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGgpsvtag 759
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGG------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 760 vPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKrAGAFDAVPCYHWSVGGKGSV 839
Cdd:pfam01268 339 -VGKDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCE-AGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 840 DLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQP 918
Cdd:pfam01268 417 ELAEAVVEACeEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 919 DKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTEtEQVKGLF 978
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
374-977 |
0e+00 |
|
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrofolate. FTHFS is a highly expressed key enzyme in both the Wood-Ljungdahl pathway of autotrophic CO2 fixation (acetogenesis) and the glycine synthase/reductase pathways of purinolysis. The key physiological role of this enzyme in acetogens is to catalyze the formylation of tetrahydrofolate, an initial step in the reduction of carbon dioxide and other one-carbon precursors to acetate. In purinolytic organisms, the enzymatic reaction is reversed, liberating formate from 10-formyltetrahydrofolate with concurrent production of ATP.
Pssm-ID: 349750 Cd Length: 540 Bit Score: 935.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 374 VDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 453
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 454 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvplvngvrefs 533
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 534 eiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIM 613
Cdd:cd00477 139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 614 AVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 693
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 694 ADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGvplkkeytEENIQL 773
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 774 VADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVpCYHWSVGGKGSVDLARAVREAASK-R 852
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKpK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 853 SRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFILPIS 932
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 36796743 933 DVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVKGL 977
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDID-DTGKIEGL 540
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
352-977 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 924.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 352 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 431
Cdd:PTZ00386 8 KLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 432 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 511
Cdd:PTZ00386 88 TTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 512 TQTDKALYNRLVplvNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQ 591
Cdd:PTZ00386 168 TQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 592 GNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLE 671
Cdd:PTZ00386 245 GKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 672 GTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHG 751
Cdd:PTZ00386 325 GTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 752 GGPSVTAGvplkkeytEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELA-KRAGAFDAVPCYH 830
Cdd:PTZ00386 405 GVEPVVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELAlQEGGAADVVVTDH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 831 WSVGGKGSVDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAK 909
Cdd:PTZ00386 477 WAKGGAGAVDLAQALIRVTeNVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAK 556
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 36796743 910 THLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGL 977
Cdd:PTZ00386 557 TQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
359-978 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 877.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 359 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 438
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 439 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 518
Cdd:COG2759 81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 519 ynrlvplvngvrefseiqlarlkklginktdpstlteeevskfaRLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGH 598
Cdd:COG2759 153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 599 YRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 678
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 679 AGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvta 758
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKL-AD--YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 759 gvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKGS 838
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 839 VDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQ 917
Cdd:COG2759 417 EELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 36796743 918 PDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVKGLF 978
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
358-978 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 748.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 358 PVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLV 437
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 438 QALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdka 517
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 518 lynrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKG 597
Cdd:PRK13505 155 ----------------------------------------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 598 HYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFV 677
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 678 HAGPFANIAHGNSSVLADKIALKLvGEegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPsvt 757
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL-AD--YVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVA--- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 758 agvplKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAfDAVPCYHWSVGGKG 837
Cdd:PRK13505 343 -----KDDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 838 SVDLARAVREAA-SKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSH 916
Cdd:PRK13505 417 GVELAEKVVELIeEGESNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 36796743 917 QPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDtETEQVKGLF 978
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVD-EDGNIVGLF 557
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
361-977 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 716.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 361 SDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQAL 440
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 441 tAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkalyn 520
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHEQ--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 521 RLvplvnGVREFseiqlarlkklginktdpstlteEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYR 600
Cdd:PRK13506 153 RL-----GYDAF-----------------------EAQSGLPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 601 QAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAG 680
Cdd:PRK13506 205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 681 PFANIAHGNSSVLADKIALKLVGeegFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGV 760
Cdd:PRK13506 285 PFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 761 PLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSVGGKGSVD 840
Cdd:PRK13506 362 ALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGATA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 841 LARAVREAASKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDK 920
Cdd:PRK13506 442 LAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPAL 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 36796743 921 KGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVkGL 977
Cdd:PRK13506 522 KGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDIDADGEIV-GL 577
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
372-978 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 662.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 372 KAVDVLAKEIGLLADEIEIYGKSKAKVR-LSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALtAHLNVNSFA 450
Cdd:PRK13507 22 KPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGL-GKRGKKVSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 451 CLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTQTDKalynrlvplvngvr 530
Cdd:PRK13507 101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDE-------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 531 efseiQLARlkklginktdpstlteeevSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVAS 610
Cdd:PRK13507 167 -----QLAR-------------------RGLKRLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 611 EIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNS 690
Cdd:PRK13507 223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 691 SVLADKIALKLvgeEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGVPLKKEYTEEN 770
Cdd:PRK13507 303 SIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 771 IQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPcYHWSVGGKGSVDLARAVREAAS 850
Cdd:PRK13507 380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 851 KRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQG-FGNLPICMAKTHLSLSHQPDKKGVPRDFIL 929
Cdd:PRK13507 459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLESDPeTADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 36796743 930 PISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGLF 978
Cdd:PRK13507 539 PIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
193-335 |
8.49e-67 |
|
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NAD(P) binding domains of methylene-tetrahydrofolate dehydrogenase (m-THF DH) and m-THF DH/cyclohydrolase bifunctional enzymes (m-THF DH/cyclohydrolase). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, mono-functional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express a monofunctional DH. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133451 Cd Length: 140 Bit Score: 220.07 E-value: 8.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 193 GDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSP 272
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 36796743 273 KPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 335
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
183-338 |
2.07e-35 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 131.82 E-value: 2.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 183 TDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLH 262
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 263 EADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHF--------------GGlieeddVILLAAALRIQ 328
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGD--VDFenvkekasaitpvpGG------VGPMTVAMLLQ 150
|
170
....*....|
gi 36796743 329 NMVSSGRRWL 338
Cdd:pfam02882 151 NTVEAAKRQL 160
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
97-289 |
3.56e-33 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 129.75 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 97 KPVLAIIQAGDD--------NLmqeinQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ------ISE 162
Cdd:COG0190 32 TPGLAVVLVGDDpasqvyvrNK-----HKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 163 NlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAhgSLE-----AALq 237
Cdd:COG0190 107 E----AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVGR--SNIvgkplALL- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 36796743 238 cLFQRKGSMTM--SiqwKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 289
Cdd:COG0190 178 -LLRRNATVTVchS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
52-290 |
1.45e-25 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 109.28 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 52 PQDGQARSSCSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFK------PVLAIIQAGDDNLMQEINQN---LAEEA 122
Cdd:PLN02897 35 PENWIPYSDPPPPVSFETEQKTVVIDGNVIAEEIRTKIASEVRKMKkavgkvPGLAVVLVGQQRDSQTYVRNkikACEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 123 GLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFV 200
Cdd:PLN02897 115 GIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 201 SPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLT 280
Cdd:PLN02897 195 SCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGS 274
|
250
....*....|
gi 36796743 281 WIQPGTTVLN 290
Cdd:PLN02897 275 WLKPGAVVID 284
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
71-290 |
4.52e-25 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 108.17 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 71 RDSIVREVIQnSKEVLSLLqeknpafkPVLAIIQAGD--DNLMQEINQNLA-EEAGLNITHICLPPDSSEAEIIDEILKI 147
Cdd:PLN02616 86 RDEITIEVSR-MKESIGVV--------PGLAVILVGDrkDSATYVRNKKKAcDSVGINSFEVRLPEDSTEQEVLKFISGF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 148 NEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILV 225
Cdd:PLN02616 157 NNDPSVHGILVQLPlpSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNVEIKGKRAVV 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 36796743 226 VGAHG--SLEAALqcLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PLN02616 237 IGRSNivGMPAAL--LLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVID 301
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
65-290 |
4.98e-25 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 106.25 E-value: 4.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 65 GRTPAARdsiVREviQNSKEVLSLlqeKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEII 141
Cdd:PRK14190 8 GKEVAKE---KRE--QLKEEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 142 DEILKINEDTRVHGLALQ------ISENlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSG 215
Cdd:PRK14190 80 ALIDRLNADPRINGILVQlplpkhIDEK----AVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 36796743 216 VNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14190 154 IDISGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
98-290 |
1.44e-24 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 104.97 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 98 PVLAIIQAG---DDNLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 172
Cdd:PLN02516 40 PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVHGILVQLPlpKHINEEKILNE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 252
Cdd:PLN02516 120 ISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHS 199
|
170 180 190
....*....|....*....|....*....|....*...
gi 36796743 253 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PLN02516 200 RTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
98-290 |
1.15e-23 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 102.21 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 98 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 172
Cdd:PRK14187 33 PCLIVILVGDDPASQlyvRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQlpVPNHIDKNLIINT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 252
Cdd:PRK14187 113 IDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVHS 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 36796743 253 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14187 193 ATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
97-300 |
1.59e-23 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 101.40 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 97 KPVLAIIQAGDD--NLMQEINQN-LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK14172 32 IPKIASILVGNDggSIYYMNNQEkVANSLGIDFKKIKLDESISEEDLINEIEELNKDNNVHGIMLQlpLPKHLDEKKITN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 172 ALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 251
Cdd:PRK14172 112 KIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIEGKEVVVIGRSNIVGKPVAQLLLNENATVTICH 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 36796743 252 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV 300
Cdd:PRK14172 190 SKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNGKI 238
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
74-274 |
9.88e-22 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 96.52 E-value: 9.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 74 IVREVIQNSKEVLSLLQEKnpAFKPVLAIIQAGDDNLMQEI---NQNLAEEAGLNITHICLPPDSSEAEIIDEILKINED 150
Cdd:PRK14175 11 IAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYvrsKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNND 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 151 TRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVG- 227
Cdd:PRK14175 89 DSVSGILVQVPlpKQVSEQKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADIDLEGKNAVVIGr 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 36796743 228 AHGSLEAALQCLFQRKGSMTMsIQWKTRQLQSKLHEADIVVLGSPKP 274
Cdd:PRK14175 167 SHIVGQPVSKLLLQKNASVTI-LHSRSKDMASYLKDADVIVSAVGKP 212
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
97-290 |
2.55e-21 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 95.61 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 97 KPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK14167 31 TPGLATVLMSDDPASEtyvSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADEDVHGILVQmpVPDHVDDREVLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 172 ALKPEKDVDGVTDINLGKLVRGDAHecFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRK---GSMTM 248
Cdd:PRK14167 111 RIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDTEGADVVVVGRSDIVGKPMANLLIQKadgGNATV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 36796743 249 SI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14167 189 TVcHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVID 231
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
82-319 |
1.02e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 93.60 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 82 SKEVLSLLQEKNpafKPVLAIIQAGDDNLMQEI---NQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLAL 158
Cdd:PRK14170 19 TREVAELVKEGK---KPGLAVVLVGDNQASRTYvrnKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDKTIHGILV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 159 Q--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSL-EAA 235
Cdd:PRK14170 96 QlpLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGK--DSFVPCTPAGIIELIKSTGTQIEGKRAVVIGRSNIVgKPV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 236 LQCLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHFGGLIEE 315
Cdd:PRK14170 174 AQLLLNENATVTIA-HSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLCGD--VDFDDVVEE 250
|
....
gi 36796743 316 DDVI 319
Cdd:PRK14170 251 AGFI 254
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
98-314 |
1.37e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 92.99 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 98 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 172
Cdd:PRK14192 34 PILATILVGDDPASAtyvRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEELNANPDVHGILLQhpVPAQIDERACFDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 173 LKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAAL-QCLFQRKGSMTMSiQ 251
Cdd:PRK14192 114 ISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYNIELAGKHAVVVGRSAILGKPMaMMLLNANATVTIC-H 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 36796743 252 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCS-HDFLSGKVGcgspRIHFGGLIE 314
Cdd:PRK14192 191 SRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGfHPRDGGGVG----DIELQGIEE 250
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
97-289 |
2.16e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 92.67 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 97 KPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK10792 33 APGLAVVLVGSDPASQVYVASkrkACEEVGFVSRSYDLPETTSEAELLALIDELNADPTIDGILVQlpLPAHIDNVKVLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 172 ALKPEKDVDGVTDINLGKLvrgdaheCFVSPV-----AKAVIELLEKSGVNLDGKKILVVGAHG------SLEAALqclf 240
Cdd:PRK10792 113 RIHPDKDVDGFHPYNVGRL-------AQRIPLlrpctPRGIMTLLERYGIDTYGLNAVVVGASNivgrpmSLELLL---- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 36796743 241 qrKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 289
Cdd:PRK10792 182 --AGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVI 228
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
131-290 |
3.62e-20 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 92.05 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 131 LPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVakAVI 208
Cdd:PRK14186 69 LPADTSQAEVEALIAQLNQDERVDGILLQlpLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPA--GVM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 209 ELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTV 288
Cdd:PRK14186 147 RLLRSQQIDIAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVV 226
|
..
gi 36796743 289 LN 290
Cdd:PRK14186 227 VD 228
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
95-300 |
3.55e-19 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 88.93 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 95 AFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKV 169
Cdd:PRK14180 29 AITPKLVAIIVGNDPASKtyvASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPlpAHINKNNV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 170 LNALKPEKDVDGVTDINLGKLVRGDaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSL-EAALQCLFQRKGSMTM 248
Cdd:PRK14180 109 IYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEGAYAVVVGASNVVgKPVSQLLLNAKATVTT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 36796743 249 SIQWkTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV 300
Cdd:PRK14180 188 CHRF-TTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDGKI 238
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
97-290 |
5.11e-19 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 88.59 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 97 KPVLAIIQAGDDNLMQEINQNLA---EEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK14189 32 QPGLAVILVGDNPASQVYVRNKVkacEDNGFHSLKDRYPADLSEAELLARIDELNRDPKIHGILVQlpLPKHIDSHKVIE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 172 ALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 251
Cdd:PRK14189 112 AIAPEKDVDGFHVANAGALMTG--QPLFRPCTPYGVMKMLESIGIPLRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICH 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 36796743 252 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14189 190 SKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVID 228
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
98-290 |
5.38e-19 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 88.72 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 98 PVLAIIQAGDDNLMQEINQNLAE---EAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 172
Cdd:PRK14174 32 PGLTVIIVGEDPASQVYVRNKAKsckEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHGILVQqpLPKQIDEFAVTLA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAH---GSLEAALQCLFQRKGSMTMS 249
Cdd:PRK14174 112 IDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKGKHCVVVGRSnivGKPMANLMLQKLKESNCTVT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 36796743 250 I-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14174 192 IcHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVID 233
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
65-290 |
2.72e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 86.82 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 65 GRTPAARdsivreVIQNSKEVLSLLqeKNPAFKPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEII 141
Cdd:PRK14194 9 GKAAAAR------VLAQVREDVRTL--KAAGIEPALAVILVGNDPASQVYVRNkilRAEEAGIRSLEHRLPADTSQARLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 142 DEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAhecFVSPVAKA-VIELLEKSGVNL 218
Cdd:PRK14194 81 ALIAELNADPSVNGILLQlpLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRD---VLTPCTPSgCLRLLEDTCGDL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 36796743 219 DGKKILVVGAH---GSLEAALqcLFQRKGSMTMsIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14194 158 TGKHAVVIGRSnivGKPMAAL--LLQAHCSVTV-VHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVID 229
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
98-290 |
3.51e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 85.97 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 98 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 172
Cdd:PRK14191 32 PKLAVILVGKDPASQtyvNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQNIDGILVQLPlpRHIDTKMVLEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 173 LKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 252
Cdd:PRK14191 112 IDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKHYHIEIKGKDVVIIGASNIVGKPLAMLMLNAGASVSVCHI 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 36796743 253 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14191 190 LTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVD 227
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
75-301 |
4.95e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 85.41 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 75 VREVIQNskEVLSLLQEKNPAFK--PVLAIIQAGDdNLMQEINQNL----AEEAGLNITHICLPPDSSEAEIIDEILKIN 148
Cdd:PRK14177 11 LSEKIRN--EIRETIEERKTKNKriPKLATILVGN-NPASETYVSMkvkaCHKVGMGSEMIRLKEQTTTEELLGVIDKLN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 149 EDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVV 226
Cdd:PRK14177 88 LDPNVDGILLQhpVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGV--ETYLPCTPYGMVLLLKEYGIDVTGKNAVVV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 36796743 227 GAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDflSGKVG 301
Cdd:PRK14177 166 GRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGNVG 238
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
131-290 |
5.69e-18 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 85.70 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 131 LPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVI 208
Cdd:PRK14168 70 QSVDITEEELLALIDKYNNDDSIHGILVQlpLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 209 ELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKG----SMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQP 284
Cdd:PRK14168 150 EMLVRSGVETSGAEVVVVGRSNIVGKPIANMMTQKGpganATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKP 229
|
....*.
gi 36796743 285 GTTVLN 290
Cdd:PRK14168 230 GATVID 235
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
90-180 |
1.50e-17 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 79.37 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 90 QEKNPAFKPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENL 164
Cdd:pfam00763 20 ALKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlpLPKHI 99
|
90
....*....|....*.
gi 36796743 165 FSNKVLNALKPEKDVD 180
Cdd:pfam00763 100 DEEKVLEAIDPEKDVD 115
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
91-290 |
1.50e-17 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 84.09 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 91 EKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLF 165
Cdd:PRK14176 32 KSNRGITPGLATILVGDDPASKmyvRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRKDVHGILLQLPlpKHLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 166 SNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGS 245
Cdd:PRK14176 112 PQEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEEYGVDIEGKNAVIVGHSNVVGKPMAAMLLNRNA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 36796743 246 MTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14176 190 TVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFD 234
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
97-289 |
1.91e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 83.85 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 97 KPVLAIIQAGDDNLMQEINQN---LAEEAGLN-ITHIcLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVL 170
Cdd:PRK14188 32 TPGLAVVLVGEDPASQVYVRSkgkQTKEAGMAsFEHK-LPADTSQAELLALIARLNADPAIHGILVQlpLPKHLDSEAVI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 171 NALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAH---GSLEAALqcLFQRKGSMT 247
Cdd:PRK14188 111 QAIDPEKDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHGDLSGLNAVVIGRSnlvGKPMAQL--LLAANATVT 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 36796743 248 MSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 289
Cdd:PRK14188 187 IA-HSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVI 227
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
69-290 |
2.82e-17 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 83.14 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 69 AARDSIVREViqnsKEVLSLLQEKnpAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEIL 145
Cdd:PRK14193 10 ATADEIKADL----AERVAALKEK--GITPGLGTVLVGDDPGSQayvRGKHRDCAEVGITSIRRDLPADATQEELNAVID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 146 KINEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPvaKAVIELLEKSGVNLDGKKI 223
Cdd:PRK14193 84 ELNADPACTGYIVQLPlpKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTP--RGIVHLLRRYDVELAGAHV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 36796743 224 LVVGAHGSLEAALQCLFQRKG-SMTMSI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14193 162 VVIGRGVTVGRPIGLLLTRRSeNATVTLcHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLD 230
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
82-303 |
6.87e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 82.20 E-value: 6.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 82 SKEVLSLLQEK--NPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGL 156
Cdd:PRK14178 9 SEKRLELLKEEiiESGLYPRLATVIVGDDPASQmyvRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 157 ALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPvaKAVIELLEKSGVNLDGKKILVVGAH---GS 231
Cdd:PRK14178 89 LVQLPlpKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTP--NGIMTLLHEYKISIAGKRAVVVGRSidvGR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 36796743 232 LEAALqcLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVgCG 303
Cdd:PRK14178 167 PMAAL--LLNADATVTIC-HSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNGKL-CG 234
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
175-291 |
8.01e-17 |
|
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains.
Pssm-ID: 133448 Cd Length: 168 Bit Score: 79.14 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 175 PEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKT 254
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKT 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 36796743 255 RQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNC 291
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDV 115
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
83-290 |
8.40e-17 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 81.72 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 83 KEVLSLLQEKnpAFKPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ 159
Cdd:PRK14179 20 EKVAKLKEEK--GIVPGLVVILVGDNPASQVYVRNkerSALAAGFKSEVVRLPETISQEELLDLIERYNQDPTWHGILVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 160 --ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAAL- 236
Cdd:PRK14179 98 lpLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSG--RPVMIPCTPAGIMEMFREYNVELEGKHAVVIGRSNIVGKPMa 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 36796743 237 QCLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14179 176 QLLLDKNATVTLT-HSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVID 228
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
83-290 |
7.50e-16 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 79.05 E-value: 7.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 83 KEVLSLLQEKNPAfkPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ 159
Cdd:PRK14184 19 TEVAALTARHGRA--PGLAVILVGEDPASQVYVRNkerACEDAGIVSEAFRLPADTTQEELEDLIAELNARPDIDGILLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 160 IS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQ 237
Cdd:PRK14184 97 LPlpKGLDSQRCLELIDPAKDVDGFHPENMGRLALG--LPGFRPCTPAGVMTLLERYGLSPAGKKAVVVGRSNIVGKPLA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 36796743 238 CLFQRKGSM---TMSI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14184 175 LMLGAPGKFanaTVTVcHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVD 231
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
97-290 |
7.50e-15 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 76.21 E-value: 7.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 97 KPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 171
Cdd:PRK14182 30 QTGLTVVRVGDDpasAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADPAVHGILVQLPlpKHVDERAVLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 172 ALKPEKDVDGVTDINLGKL---VRGDAHECfvspVAKAVIELLEKSGVNLDGKKILVVGAH---GSLEAALqcLFQRKGS 245
Cdd:PRK14182 110 AISPAKDADGFHPFNVGALsigIAGVPRPC----TPAGVMRMLDEARVDPKGKRALVVGRSnivGKPMAMM--LLERHAT 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 36796743 246 MTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14182 184 VTIA-HSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVID 227
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
73-298 |
4.46e-14 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 73.84 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 73 SIVREVIQNSKEVLSLLQEKNPAfKPVLAIIQAGDDN-----LMQEINQnlAEEAGLNITHICLPPDSSEAEIIDEILKI 147
Cdd:PRK14171 9 ALANEILADLKLEIQELKSQTNA-SPKLAIVLVGDNPasiiyVKNKIKN--AHKIGIDTLLVNLSTTIHTNDLISKINEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 148 NEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdAHECFVSPVAKAVIELLEKSGVNLDGKKILV 225
Cdd:PRK14171 86 NLDNEISGIIVQLPlpSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTGKNVVI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 36796743 226 VGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSG 298
Cdd:PRK14171 165 IGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISG 237
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
82-300 |
1.39e-13 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 72.37 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 82 SKEVLSLLQEKNPAFK-----PVLAIIQAGDDNLMQEINQNLA---EEAGLNITHICLPPDSSEAEIIDEILKINEDTRV 153
Cdd:PRK14166 10 SAKIKEELKEKNQFLKskgieSCLAVILVGDNPASQTYVKSKAkacEECGIKSLVYHLNENTTQNELLALINTLNHDDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 154 HGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGS 231
Cdd:PRK14166 90 HGILVQLPlpDHICKDLILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEGKDAVIIGASNI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 232 LEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFL-SGKV 300
Cdd:PRK14166 169 VGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLeSGKI 238
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
97-290 |
1.75e-13 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 72.17 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 97 KPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 171
Cdd:PRK14185 31 RPHLAAILVGHDGGSETYVANkvkACEECGFKSSLIRYESDVTEEELLAKVRELNQDDDVDGFIVQLPlpKHISEQKVIE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 172 ALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRK---GSMTM 248
Cdd:PRK14185 111 AIDYRKDVDGFHPINVGRMSIG--LPCFVSATPNGILELLKRYHIETSGKKCVVLGRSNIVGKPMAQLMMQKaypGDCTV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 36796743 249 SI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14185 189 TVcHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVID 231
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
98-290 |
5.21e-13 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 70.66 E-value: 5.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 98 PVLAIIQAGDDNlMQEINQNLAEEAGLNITHIC----LPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 171
Cdd:PRK14181 27 PGLAVVLIGNDP-ASEVYVGMKVKKATDLGMVSkahrLPSDATLSDILKLIHRLNNDPNIHGILVQLPlpKHLDAQAILQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 36796743 172 ALKPEKDVDGVTDINLGKLVRGDAhECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMS-- 249
Cdd:PRK14181 106 AISPDKDVDGLHPVNMGKLLLGET-DGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAALLMQKHPDTNAtv 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 36796743 250 --IQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14181 185 tlLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVD 227
|
|
| |
