|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
1-432 |
0e+00 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 819.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHFFDLPDFLSWKATGVTARSLCSLVC 80
Cdd:cd07782 105 LWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHFFDLPDFLTWKATGSLTRSLCSLVC 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 81 KWTYSA----EKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAARELGLPSGIAVAASLIDAHAGGLGV 156
Cdd:cd07782 184 KWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 157 IGADVrgHGLTCEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAF 236
Cdd:cd07782 264 LGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAY 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 237 PELQAKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLA 314
Cdd:cd07782 342 PELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALLYLA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 315 TVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEA 394
Cdd:cd07782 422 TLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDA 501
|
410 420 430
....*....|....*....|....*....|....*...
gi 568929917 395 MARMSKVGKVVFPEHADKKYYDKKYQVFLRMVEHQKEY 432
Cdd:cd07782 502 MAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQREY 539
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
1-432 |
0e+00 |
|
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins.
Pssm-ID: 273552 [Multi-domain] Cd Length: 541 Bit Score: 549.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC 80
Cdd:TIGR01315 105 LWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKFFDLTDFLTWRATGKEIRSFCSVVC 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 81 KWTY----SAEKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAARELGLPSGIAVAASLIDAHAGGLGV 156
Cdd:TIGR01315 184 KWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQELGLPAGTAVGSGLIDAHAGWIGT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 157 IGADVRGHGltcEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAF 236
Cdd:TIGR01315 264 VGAKVAENG---DVSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAEGGQSAAGELMDHMLETHVAY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 237 PELQAKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILY 312
Cdd:TIGR01315 341 DETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIADPNMRGVIIGLSMDRSKDGLALLY 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 313 LATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQ 392
Cdd:TIGR01315 420 YATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAVLHGAAMLGAKAAGTTESLW 499
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 568929917 393 EAMARMSKVGKVVFP-EHADKKYYDKKYQVFLRMVEHQKEY 432
Cdd:TIGR01315 500 DAMDRMSKPGKTVWPrGDPAKKLHDRKYEIFLQLARTQQEY 540
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
1-434 |
1.07e-170 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 489.24 E-value: 1.07e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINE----TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLC 76
Cdd:COG1069 117 LWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPKILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRC 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 77 SLVCKWTYSA-EKGW-DDSFWKMIG--LEDLIDdnysKIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAG 152
Cdd:COG1069 196 TAGHKALWHAhEGGYpSEEFFAALDplLDGLAD----RLGTEIYPLGEPAG-TLTAEWAARLGLPPGTAVAVGAIDAHAG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 153 GLGVIGAdvrghgltCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQG 232
Cdd:COG1069 271 AVGAGGV--------EPGT-----LVKVMGTSTCHMLVSPEERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 233 HPAFPELQAKATARCQSIYAYLNshldliKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLY 312
Cdd:COG1069 338 LVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IY 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 313 LATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSV 391
Cdd:COG1069 409 RALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDV 488
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 568929917 392 QEAMARMSKV-GKVVFPEHADKKYYDKKYQVFLRMVEHQKEYSA 434
Cdd:COG1069 489 EEAMAAMGSGfDKVYTPDPENVAVYDALYAEYLQLHDYFGRGRN 532
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
1-422 |
1.01e-125 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 374.27 E-value: 1.01e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINETKHRVLQ-YVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLV 79
Cdd:cd07768 107 FWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKHFHIFDLHDYIAYELTRLYEWNICGLL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 80 CKWTYSA-EKGWDDSFWKMIGLEDLiDDNYSKIGNLVLLPGAALGIGLtPEAARELGLPSGIAVAASLIDAHAGGLGVIG 158
Cdd:cd07768 186 GKENLDGeESGWSSSFFKNIDPRLE-HLTTTKNLPSNVPIGTTSGVAL-PEMAEKMGLHPGTAVVVSCIDAHASWFAVAS 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 159 ADVRGhgltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPE 238
Cdd:cd07768 264 PHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATGKLIEHLFESHPCARK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 239 LQaKATARCQSIYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQA 318
Cdd:cd07768 332 FD-EALKKGADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLNLTYKYIAILEA 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 319 IAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFT---SVQEAM 395
Cdd:cd07768 408 LAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQladSITEAD 487
|
410 420
....*....|....*....|....*...
gi 568929917 396 ARMSKVGKVVFPE-HADKKYYDKKYQVF 422
Cdd:cd07768 488 ISNDRKSETFEPLaYRLGADYILLYKLL 515
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
1-425 |
2.90e-120 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 359.54 E-value: 2.90e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINETKHRV----LQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLC 76
Cdd:cd07781 100 LWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV-YDAAYTIVEACDWINARLTGRWVRSRC 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 77 SLVCKWTYSAEKG-WDDSFWKMIGLEDLidDNYSKIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGglg 155
Cdd:cd07781 179 AAGHKWMYNEWGGgPPREFLAALDPGLL--KLREKLPGEVVPVGEPAG-TLTAEAAERLGLPAGIPVAQGGIDAHMG--- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 156 VIGADVRGHGltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDhmvqghpA 235
Cdd:cd07781 253 AIGAGVVEPG----------TLALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGLYGLEAGQSAVGDIFA-------W 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 236 FPELQAKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLddlAILY 312
Cdd:cd07781 316 FVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNRTPLVDPRLRGAIVGLTLGTTP---AHIY 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 313 LATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSV 391
Cdd:cd07781 385 RALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADI 464
|
410 420 430
....*....|....*....|....*....|....
gi 568929917 392 QEAMARMSKVGKVVFPEHADKKYYDKKYQVFLRM 425
Cdd:cd07781 465 EEAADAMVRVDRVYEPDPENHAVYEELYALYKEL 498
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
2-436 |
2.33e-73 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 239.75 E-value: 2.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 2 WLDHRAVSQVHRINETKHR-----VLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA---- 72
Cdd:PRK04123 119 WKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKILHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdi 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 73 -RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDLIDDnysKIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLI 147
Cdd:PRK04123 198 vRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD---KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAF 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 148 DAHAGglgVIGADVRGHGLTcegqpvtsrlAVIcGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKL-- 225
Cdd:PRK04123 274 DAHMG---AVGAGAEPGTLV----------KVM-GTSTCDILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIfa 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 226 --IDHMVQghpafPELQAKATARCQSIYAYLNshldliKKA--QPVG---FLTVDlhvWpdFHGNRSPLADLTLKGMVTG 298
Cdd:PRK04123 340 wfARLLVP-----PEYKDEAEARGKQLLELLT------EAAakQPPGehgLVALD---W--FNGRRTPLADQRLKGVITG 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 299 LTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGA 377
Cdd:PRK04123 404 LTLGTDAPDI---YRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGA 480
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568929917 378 AILGACASGDFTSVQEAMARM-SKVGKVVFPEHADKKYYDKKYQVFLRMVE-HQKEYSAIM 436
Cdd:PRK04123 481 AIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPENVARYEQLYQEYKQLHDyFGRGGNAVM 541
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
1-431 |
1.20e-70 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 231.26 E-value: 1.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLC 76
Cdd:COG1070 98 LWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FARIAKVLLPKDYLRYRLTGefVTDYSDA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 77 SlvckWT--YSAEKG-WDDSFWKMIGLEDLIddnyskignL--VLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHA 151
Cdd:COG1070 177 S----GTglLDVRTRdWSDELLEALGIDREL---------LpeLVPPGEVAG-TLTAEAAAETGLPAGTPVVAGAGDNAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 152 GGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQ 231
Cdd:COG1070 243 AALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRD 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 232 ghpafpELQAKAtarcQSIYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLD 306
Cdd:COG1070 310 ------LFADGE----LDDYEELN---ALAAEV-PPGadgllFL-------PYLSGERTPHWDPNARGAFFGLTLSHTRA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 307 DLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 386
Cdd:COG1070 369 HL---ARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLG 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 568929917 387 DFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQVFLRMVEHQKE 431
Cdd:COG1070 446 LYDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYRELYPALKP 490
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
177-384 |
8.22e-61 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 196.39 E-value: 8.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 177 LAVICGTSSCHMGISKDPV-FVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAkaTARCQSIYAYLN 255
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRD--AGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 256 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLddlAILYLATVQAIAFGTRFIIETMEA-AG 334
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568929917 335 HSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACA 384
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
1-423 |
2.86e-59 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 202.63 E-value: 2.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINE-TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAgHFFDLPDFLSWKatgvtarsLCSLV 79
Cdd:cd07778 111 FWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTFKKL-EVFDLHDWISYM--------LATNL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 80 CKW--TYSAE------------KGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIG-LTPEAARELGLPSGIAVAA 144
Cdd:cd07778 182 GHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNVGNTFKEAPPLPYAGIPIGkVNVILASYLGIDKSTVVGH 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 145 SLIDAHAGGLGVIgadvrghgltCEGQPVTSRLAVICGTSSCHMGISKDPV--FVPGVWGPYySAMVPGFWLNEGGQSVT 222
Cdd:cd07778 262 GCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTCFLYATSSSQvgPIPGIWGPF-DQLLKNYSVYEGGQSAT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 223 GKLIDHMVQGHPAFPELQAKATarcqSIYAYLNSHLDLI--KKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLT 300
Cdd:cd07778 331 GKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerLLGQSIHYLTRHMFFYGDYLGNRTPYNDPNMSGSFIGES 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 301 LSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVV---LSQEVESVLVGA 377
Cdd:cd07778 407 TDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSTVLSKIHIivpLSDSKYAVVKGA 486
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 568929917 378 AILGACASGDFTSVQEAMARMSKVGKVVFPEHADK-----------KYYDKKYQVFL 423
Cdd:cd07778 487 ALLGKAAFLHNQSIEERLISLKNEDQISICASASIvklvsdetklaIILRAKYQIMN 543
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
1-432 |
2.15e-56 |
|
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli. [Energy metabolism, Sugars]
Pssm-ID: 130301 [Multi-domain] Cd Length: 536 Bit Score: 194.76 E-value: 2.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINETKHR----VLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLC 76
Cdd:TIGR01234 121 LWKHHAAQEEADRINRLAHApgevDLSRYGGIISSEWFWAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 77 SLVCKWTYSAEKGW-DDSFWKMI--GLEDLIDDNYSK-IGNLvllpGAALGiGLTPEAARELGLPSGIAVAASLIDAHag 152
Cdd:TIGR01234 200 TAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTdIWTA----GEPAG-TLTPEWAQRTGLPEGVVVAVGNFDAH-- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 153 gLGVIGADVrghgltceGQPvtSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQg 232
Cdd:TIGR01234 273 -VGAVAAGI--------AQP--GALVKIMGTSTCHVLIGDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 233 HPAFPELQAKATARCQSiyayLNSHLDLIKKAQPV---GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDla 309
Cdd:TIGR01234 341 VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgehGLVALD---W--FNGNRSPLVDQRLKGVITGLTLATDAPL-- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 310 iLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDF 388
Cdd:TIGR01234 410 -LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIArKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVY 488
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 568929917 389 TSVQEAMARMSKVGKVVF---PEHADKkyYDKKYQVFLRMVEHQKEY 432
Cdd:TIGR01234 489 ADIPSAQAKMGSAVEKTLtpcSENAQR--YEQLYARYQELAMSFGQY 533
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
48-415 |
2.17e-53 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 184.26 E-value: 2.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 48 ICW-DK-AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDliddnySKIGNLVLlPGAALGi 124
Cdd:cd07779 96 ISWqDKrTAKFLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGIDR------DKLPELVP-PGTVIG- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 125 GLTPEAARELGLPSGIAVAASlidAHAGGLGVIGAdvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPY 204
Cdd:cd07779 168 TLTKEAAEETGLPEGTPVVAG---GGDQQCAALGA-----GVLEPGT-----ASLSLGTAAVVIAVSDKPVEDPERRIPC 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 205 YSAMVPGFWLNEGGQSVTGKLIDHMVQghpAFPELQAKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNR 284
Cdd:cd07779 235 NPSAVPGKWVLEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 285 SPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPV 364
Cdd:cd07779 306 TPYWNPEARGAFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPV 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568929917 365 VLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYY 415
Cdd:cd07779 383 ERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
1-425 |
7.91e-52 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 181.20 E-value: 7.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINET-KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFdLP-DFLSWKATGVTAR----- 73
Cdd:cd07808 97 LWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIRKIL-LPkDYLRYRLTGELATdpsda 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 74 --SLCslvckwtYSAEKG-WDDSFWKMIGLEdliddnyskIGNL--VLLPGAALGiGLTPEAARELGLPSGIAVAASLID 148
Cdd:cd07808 175 sgTLL-------FDVEKReWSEELLEALGLD---------PSILppIVESTEIVG-TLTPEAAEELGLPEGTPVVAGAGD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 149 AHAGGLGVigadvrghGLTCEGQPV----TSrlAVICGTSSCHMGISKDPVF-----VPGVWgpYYSAMVPGF-----WL 214
Cdd:cd07808 238 NAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtfphaVPGKW--YAMGVTLSAglslrWL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 215 NE--GGQSVTGKLIDHMVQGHPAfpelqakatarcqsiyaylnshldlikKAQPVGFLtvdlhvwPDFHGNRSPLADLTL 292
Cdd:cd07808 306 RDlfGPDRESFDELDAEAAKVPP---------------------------GSEGLLFL-------PYLSGERTPYWDPNA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 293 KGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVES 372
Cdd:cd07808 352 RGSFFGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEG 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 568929917 373 VLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQVFLRM 425
Cdd:cd07808 429 SAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
1-423 |
1.38e-51 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 180.79 E-value: 1.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINETKHRVLQY---VGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCS 77
Cdd:cd07805 97 IWSDTRAAEEAEEIAGGLGGIEGYrlgGGNPPSGKDPLAKILWLKENEPEI-YAKTHKFLDAKDYLNFRLTGRAATDPST 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 78 LVCKWTYSAEKG-WDDSFWKMIGLE-DLIDDnyskignlvLLPGAALgIG-LTPEAARELGLPSGIAVAASLIDAHAGGL 154
Cdd:cd07805 176 ASTTGLMDLRKRrWSEELLRAAGIDpDKLPE---------LVPSTEV-VGeLTPEAAAELGLPAGTPVVGGGGDAAAAAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 155 GViGADVRGHgltcegqpvtsrlAVIC-GTSS---CHmgiSKDPVFVPGvwGPYYS--AMVPGFWLNEGGQSVTGKLIDH 228
Cdd:cd07805 246 GA-GAVEEGD-------------AHIYlGTSGwvaAH---VPKPKTDPD--HGIFTlaSADPGRYLLAAEQETAGGALEW 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 229 MVqghpafpELQAKATARCQSIYAYLNshlDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQD 304
Cdd:cd07805 307 AR-------DNLGGDEDLGADDYELLD---ELAAEAPPgsngLLFL-------PWLNGERSPVEDPNARGAFIGLSLEHT 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 305 LDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPV-VLSQEVESVLVGAAILGAC 383
Cdd:cd07805 370 RADLA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVeVPENPQEAGALGAALLAAV 446
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 568929917 384 ASGDFTSVQEAmARMSKVGKVVFPEHADKKYYDKKYQVFL 423
Cdd:cd07805 447 GLGLLKSFDEA-KALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
1-386 |
6.00e-43 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 156.59 E-value: 6.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLcSL 78
Cdd:cd07773 95 VWFDPRGKEEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAAKWLSVADYIAYRLTGEPVTDY-SL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 79 VCKWTY--SAEKGWDDSfwkmigLEDLIDDNYSKIGNLVLlPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAGGLGV 156
Cdd:cd07773 173 ASRTMLfdIRKRTWSEE------LLEAAGIDASLLPELVP-SGTVIGT-VTPEAAEELGLPAGTPVVVGGHDHLCAALGA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 157 igadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYS---AMVPGFWLNEGGQSvTGKLIDHMVQgh 233
Cdd:cd07773 245 --------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVPGGYYYLAGSLP-GGALLEWFRD-- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 234 pafpELQAKATARCQSIYAYLNShldlIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLailYL 313
Cdd:cd07773 309 ----LFGGDESDLAAADELAEAA----PPGPTGLLFL-------PHLSGSGTPDFDPDARGAFLGLTLGTTRADL---LR 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568929917 314 ATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 386
Cdd:cd07773 371 AILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
1-386 |
6.32e-42 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 153.84 E-value: 6.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLC 76
Cdd:cd07804 97 LYGDRRATEEIEWLNENigEDRIFEITGNPLDSQSVGPKLLWIKRNEPEV-FKKTRKFLGAYDYIVYKLTGeyVIDYSSA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 77 SLvckwtYS-----AEKGWDDSFWKMIGL-EDLIDDNYSkignlvllPGAALGiGLTPEAARELGLPSGIAVAASLIDAH 150
Cdd:cd07804 176 GN-----EGglfdiRKRTWDEELLEALGIdPDLLPELVP--------STEIVG-EVTKEAAEETGLAEGTPVVAGTVDAA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 151 AGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYSamVPGFWLNEGGQSVTGKLIDHMV 230
Cdd:cd07804 242 ASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRLWLDYHD--IPGTYVLNGGMATSGSLLRWFR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 231 QGhpAFPELQAKATARCQSIYAYLNshldliKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLai 310
Cdd:cd07804 307 DE--FAGEEVEAEKSGGDSAYDLLD------EEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHL-- 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568929917 311 lYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 386
Cdd:cd07804 377 -YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
51-381 |
1.38e-41 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 151.56 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 51 DKAGHFFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGLEDliddnySKIGNLVLlPGAALGiGLTP 128
Cdd:cd00366 100 DRRAKFLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIPR------EKLPPIVE-SGEVVG-RVTP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 129 EAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVtsrlaVICGTSSCHMGISKDPVFVPGVWGPYYSAm 208
Cdd:cd00366 171 EAAEETGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 209 VPGFWLNEGGQSVTGKLIDHMvqghpafpelqAKATARCQSIYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGNR 284
Cdd:cd00366 237 VPGLWLLEGAINTGGASLRWF-----------RDEFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGER 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 285 SPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPV 364
Cdd:cd00366 299 SPIWDPAARGVFFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPV 375
|
330
....*....|....*..
gi 568929917 365 VLSQEVESVLVGAAILG 381
Cdd:cd00366 376 VVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
1-386 |
1.74e-39 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 147.31 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsL 78
Cdd:cd07802 97 LSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRIRTVLFCKDWIRYRLTGE-------I 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 79 VCKWT-YSA------EKGWDDSFWKMIGLEDLIDdnysKIGNLVllPGAALGIGLTPEAARELGLPSGIAVAASLIDAHA 151
Cdd:cd07802 169 STDYTdAGSslldldTGEYDDELLDLLGIEELKD----KLPPLV--PSTEIAGRVTAEAAALTGLPEGTPVAAGAFDVVA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 152 GGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGpYYSAMVPGFWLNEGGQSVTGKLIDHMVQ 231
Cdd:cd07802 243 SALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSLHADPGLYLIVEASPTSASNLDWFLD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 232 ghpafpELQAKATARCQSIYAYLNshlDLIKKAQPVG----FLtvdlhvwPDFHGNRsplADLTLKGMVTGLTLSQDLDD 307
Cdd:cd07802 309 ------TLLGEEKEAGGSDYDELD---ELIAAVPPGSsgviFL-------PYLYGSG---ANPNARGGFFGLTAWHTRAH 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929917 308 LAilyLATVQAIAFGTRFIIETMEAAGHsLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 386
Cdd:cd07802 370 LL---RAVYEGIAFSHRDHLERLLVARK-PETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
1-382 |
2.33e-39 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 146.60 E-value: 2.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC 80
Cdd:cd07783 95 MYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFLHQADWLAGRLTGDRGVTDYNNAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 81 KWTYSAEKG-WDDSFWKMIGL-EDLIddnyskigNLVLLPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAGGLGViG 158
Cdd:cd07783 174 KLGYDPETGrWPSWLLALLGIpPDLL--------PRVVAPGTVIGT-LTAEAAEELGLPAGTPVVAGTTDSIAAFLAS-G 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 159 ADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDPVFVPGvwGPYYSAMVP-GFWLNEGGQSVTGKLIDHMVQGHPaFP 237
Cdd:cd07783 244 AVRPGDAVT------------SLGTTLVLKLLSDKRVPDPG--GGVYSHRHGdGYWLVGGASNTGGAVLRWFFSDDE-LA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 238 ELQAKATARCQSiyaylnshldlikkaqpvgfltvDLHVWP-DFHGNRSPLADLTLKGMVTGLTlsqdlDDLAILYLATV 316
Cdd:cd07783 309 ELSAQADPPGPS-----------------------GLIYYPlPLRGERFPFWDPDARGFLLPRP-----HDRAEFLRALL 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568929917 317 QAIAFGTRFIIETMEAAGHS-LSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLvGAAILGA 382
Cdd:cd07783 361 EGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAAL-GAALLAA 426
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
2-426 |
5.04e-37 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 141.15 E-value: 5.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 2 WLDHRAVSQVHRI--NETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATG--VTARSLCS 77
Cdd:cd07770 96 WADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAKFVSIKEYLLYRLTGelVTDYSTAS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 78 lvckWT---YSAEKGWDDSFWKMIGLEDlidDNYSKignlvLLPGAALGIGLTPEAARELGLPSGIAVAASLIDAHAGGL 154
Cdd:cd07770 175 ----GTgllNIHTLDWDEEALELLGIDE---EQLPE-----LVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGALANL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 155 GViGADVRGhgltcegqpvtsRLAVICGTSschmG----ISKDPVFVP--GVWgPYYSAmvPGFWL-----NEGGqSVTG 223
Cdd:cd07770 243 GS-GALDPG------------RAALTVGTS----GairvVSDRPVLDPpgRLW-CYRLD--ENRWLvggaiNNGG-NVLD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 224 KLIDHMVQGHPAFPELQAKATArcqsiyAYLNSHlDLIkkaqpvgFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQ 303
Cdd:cd07770 302 WLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PYLAGERAPGWNPDARGAFFGLTLNH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 304 DLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGAC 383
Cdd:cd07770 361 TRADI---LRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALE 437
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568929917 384 ASGDFTSVQEamARMSKVGKVVFPEHADKKYYDKKYQVFLRMV 426
Cdd:cd07770 438 ALGLISSLEA--DELVKIGKVVEPDPENHAIYAELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-386 |
2.46e-30 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 121.95 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 4 DHRAVSQVHRINETKHRVLQYVGGVMSVEMQAP-KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKW 82
Cdd:cd07798 101 DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRPEI-FERIATVLSISDWIGYRLTGE-------LVSEP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 83 TYSAEKG--------WDDSFWKMIGLEDLIddnyskignL--VLLPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAG 152
Cdd:cd07798 173 SQASETQlfdikkreWSQELLEALGLPPEI---------LpeIVPSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 153 GLGViGADVRGHgltcegqpvtsrLAVICGTSSCHMGISKDPVFVP--GVW-GPYysaMVPGFWLNEGGQSVTGKLIDHM 229
Cdd:cd07798 243 LLGS-GAIEPGD------------IGIVAGTTTPVQMVTDEPIIDPerRLWtGCH---LVPGKWVLESNAGVTGLNYQWL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 230 VQGHPAFPELQakatarcqsiYAYLNSHLDLIKKAQP--VGFLTVDLhvwpdFHGNRSPLADLTLKGMVTGLTLSQDLDD 307
Cdd:cd07798 307 KELLYGDPEDS----------YEVLEEEASEIPPGANgvLAFLGPQI-----FDARLSGLKNGGFLFPTPLSASELTRGD 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 308 LAIlylATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 386
Cdd:cd07798 372 FAR---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
25-386 |
1.60e-25 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 108.02 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 25 VGGVMSVEMQAPKLLWLKENLREIcWDKAgHFFDLP-DFLSWKATG--VTARSLCSLVckwtysaekGWDDSF-----WK 96
Cdd:cd07809 123 VGLNIPARFTASKLLWLKENEPEH-YARI-AKILLPhDYLNWKLTGekVTGLGDASGT---------FPIDPRtrdydAE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 97 MIGLEDLIDDNYSKIGNlVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAG--GLGVIGadvrghgltcEGQPVT 174
Cdd:cd07809 192 LLAAIDPSRDLRDLLPE-VLPAGEVAG-RLTPEGAEELGLPAGIPVAPGEGDNMTGalGTGVVN----------PGTVAV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 175 SrlaviCGTSSCHMGISKDPVFVPgvwgpyySAMVPGF--------WLNEG---GQSVTGKLIDHMVQGHPAFPELQAKA 243
Cdd:cd07809 260 S-----LGTSGTAYGVSDKPVSDP-------HGRVATFcdstggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 244 TARCQSIYAYlnshldlikkaqpvgfltvdlhvwPDFHGNRSP-LADLTlkGMVTGLTLSQDldDLAILYLATVQAIAFG 322
Cdd:cd07809 328 PPGAGGLLLL------------------------PFLNGERTPnLPHGR--ASLVGLTLSNF--TRANLARAALEGATFG 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568929917 323 TRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 386
Cdd:cd07809 380 LRYGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
1-386 |
4.10e-25 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 106.94 E-value: 4.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICwDKAGHFFDLPDFLSWKATGVTA--RSLC 76
Cdd:cd24121 97 LWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-ERARTALHCKDWLFYKLTGEIAtdPSDA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 77 SLVCkwtYSAEKG-WDDSFWKMIGLEDLIDdnyskignlvLLPGAALGIG----LTPEAARELGLPSGIAVAASLIDAHA 151
Cdd:cd24121 176 SLTF---LDFRTRqYDDEVLDLLGLEELRH----------LLPPIRPGTEvigpLTPEAAAATGLPAGTPVVLGPFDVVA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 152 GGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDPVFvpgvwGPYYSAM-----VPGFWLNEGGqSVTGKL- 225
Cdd:cd24121 243 TALGS-GAIEPGDACS------------ILGTTGVHEVVVDEPDL-----EPEGVGYticlgVPGRWLRAMA-NMAGTPn 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 226 IDHMVQghPAFPELQAKATARCQSIYAYLNSHLdlikKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDL 305
Cdd:cd24121 304 LDWFLR--ELGEVLKEGAEPAGSDLFQDLEELA----ASSPPGAEGVLYHPYLSPAGERAPFVNPNARAQFTGLSLEHTR 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 306 DDLAilyLATVQAIAFGTRfiiETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACAS 385
Cdd:cd24121 378 ADLL---RAVYEGVALAMR---DCYEHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVAL 451
|
.
gi 568929917 386 G 386
Cdd:cd24121 452 G 452
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-420 |
6.78e-22 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 97.79 E-value: 6.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 4 DHRAVSQVHRINETKH---RVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSL 78
Cdd:cd07775 101 DARAAEEVSELKELYNtleEEVYRISGQTFALGAIPRLLWLKNNRPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGST 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 79 VCKWTySAEKGWDDSFWKMIGLEDLIDDNyskignlVLLPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAGGLGVig 158
Cdd:cd07775 180 TGLFD-LKTRDWDPEILEMAGLKADILPP-------VVESGTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 159 advrghGLTCEGQpvtsrlAVICGTSSCHMGI-SKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQghpAF- 236
Cdd:cd07775 249 ------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD---AFc 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 237 PELQAKATARCQSIYAYLNshldliKKAQ--PVGF-----LTVDL-------HVWPDFhgnrspladltlkgmvTGLTLS 302
Cdd:cd07775 314 AEEKEIAERLGIDAYDLLE------EMAKdvPPGSygimpIFSDVmnyknwrHAAPSF----------------LNLDID 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 303 QDLDDLAILYLATVQAIAFGTRFIIETMEAA-GHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILG 381
Cdd:cd07775 372 PEKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAA 451
|
410 420 430
....*....|....*....|....*....|....*....
gi 568929917 382 ACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQ 420
Cdd:cd07775 452 GVGAGIYSSLEEAVESLVKWEREYLPNPENHEVYQDLYE 490
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
278-427 |
1.64e-16 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 81.36 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 278 PDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMH 356
Cdd:cd07769 341 PAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQ 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568929917 357 ADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEaMARMSKVGKVVFPEhADKKYYDKKYQVFLRMVE 427
Cdd:cd07769 418 ADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDE-LASLWQVDKRFEPS-MDEEERERLYRGWKKAVE 486
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
314-427 |
5.85e-16 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 79.88 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 314 ATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQ 392
Cdd:cd07792 384 AALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLD 463
|
90 100 110
....*....|....*....|....*....|....*
gi 568929917 393 EaMARMSKVGKVVFPEHADKKYYDKKYQVFLRMVE 427
Cdd:cd07792 464 E-LKSLNEGGRTVFEPQISEEERERRYKRWKKAVE 497
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
293-427 |
1.30e-15 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 78.57 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 293 KGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVE 371
Cdd:COG0554 359 RGAIFGLTRGTTRAHIA---RAALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTE 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568929917 372 SVLVGAAILGACASGDFTSVQEaMARMSKVGKVVFPEhADKKYYDKKYQVFLRMVE 427
Cdd:COG0554 436 TTALGAAYLAGLAVGFWKSLEE-LAALWKVDRRFEPQ-MDEEERERLYAGWKKAVE 489
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
278-419 |
3.29e-15 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 77.32 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 278 PDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETME-AAGHSLSTLFLCGGLSKNPLFVQMH 356
Cdd:PTZ00294 350 PAFSGLFAPYWRPDARGTIVGMTLKTTRAHIV---RAALEAIALQTNDVIESMEkDAGIELNSLRVDGGLTKNKLLMQFQ 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568929917 357 ADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPeHADKKYYDKKY 419
Cdd:PTZ00294 427 ADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRSNSTFSP-QMSAEERKAIY 488
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
293-427 |
9.67e-15 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 75.99 E-value: 9.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 293 KGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVE 371
Cdd:cd07786 356 RGAIFGLTRGTTRAHIA---RAALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTE 432
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568929917 372 SVLVGAAILGACASGDFTSVQEAmARMSKVGKVVFPEhADKKYYDKKYQVFLRMVE 427
Cdd:cd07786 433 TTALGAAYLAGLAVGLWKSLDEL-AKLWQVDRRFEPS-MSEEEREALYAGWKKAVK 486
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
278-427 |
5.92e-14 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 73.36 E-value: 5.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 278 PDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAIlylATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMH 356
Cdd:cd07793 356 PAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLI 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568929917 357 ADITGMPVVLSQEVESVLVGAAILGACASGDFTSVqEAMARMSKVGKVVFPEhADKKYYDKKYQVFLRMVE 427
Cdd:cd07793 433 ADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
275-428 |
2.95e-12 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 68.31 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 275 HVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFV 353
Cdd:PRK00047 344 YVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHII---RATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLM 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568929917 354 QMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEaMARMSKVGKVVFPEHADKKyYDKKYQVFLRMVEH 428
Cdd:PRK00047 421 QFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDE-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
37-407 |
4.06e-12 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 67.75 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 37 KLLWLKENLREIcWDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGL-EDL---IDDNYSK 110
Cdd:PRK10331 137 KLVWLKENHPQL-LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLsRRLfprLVEAGEQ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 111 IGNLvllpgaalgiglTPEAARELGLPSGIAVAASlidAHAGGLGVIGAdvrGHGLtceGQPV----------------- 173
Cdd:PRK10331 215 IGTL------------QPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVlssgtweilmvrsaqvd 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 174 TSRLAVICGtSSCHMGiSKDPVFVPGVWgpyysamvpgfWLNEGGQSVTGKLIdhmvqghpaFPELQAKATarcqsiyay 253
Cdd:PRK10331 274 TSLLSQYAG-STCELD-SQSGLYNPGMQ-----------WLASGVLEWVRKLF---------WTAETPYQT--------- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 254 lnshldLIKKAQPVGFLTVDLHVWPDFHGNRspladltlKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAA 333
Cdd:PRK10331 323 ------MIEEARAIPPGADGVKMQCDLLACQ--------NAGWQGVTLNTTRGHF---YRAALEGLTAQLKRNLQVLEKI 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568929917 334 GH-SLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFP 407
Cdd:PRK10331 386 GHfKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYFYP 460
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
1-425 |
6.77e-11 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 63.83 E-value: 6.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 1 MWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAGHFfdLP-DFLSWKATGVTARSLCSLV 79
Cdd:PRK15027 95 LWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVL--LPkDYLRLRMTGEFASDMSDAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 80 -CKWTYSAEKGWDDSfwkMIGLEDLIDDNYSkignlVLLPGAALGIGLTPEAARELGLPSgIAVAASLIDAHAGGLGVig 158
Cdd:PRK15027 173 gTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAKAWGMAT-VPVVAGGGDNAAGAVGV-- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 159 advrghGLTCEGQPVTSrlaviCGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWlneggqsvtgKLIDHMVQGHPAFpE 238
Cdd:PRK15027 242 ------GMVDANQAMLS-----LGTSGVYFAVSEGFLSKPESAVHSFCHALPQRW----------HLMSVMLSAASCL-D 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 239 LQAKATARcQSIYAYLNSHLDLIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQA 318
Cdd:PRK15027 300 WAAKLTGL-SNVPALIAAAQQADESAEPVWFL-------PYLSGERTPHNNPQAKGVFFGLTHQHGPNELA---RAVLEG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 319 IAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQ--EVESVLvGAAILGACASGDFTSVQEAMA 396
Cdd:PRK15027 369 VGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTggDVGPAL-GAARLAQIAANPEKSLIELLP 447
|
410 420
....*....|....*....|....*....
gi 568929917 397 RMSkVGKVVFPEHADKKYYDKKYQVFLRM 425
Cdd:PRK15027 448 QLP-LEQSHLPDAQRYAAYQPRRETFRRL 475
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
4-429 |
1.28e-09 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 60.02 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 4 DHRAVSQV----HRINETKHRVLQYVGGVMSVEmQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA------- 72
Cdd:PRK10939 104 DARASREVselkELHNNFEEEVYRCSGQTLALG-ALPRLLWLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsnag 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 73 -RSLCSLVckwtysaEKGWDDSFWKMIGLedlIDDNYSKignlVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHA 151
Cdd:PRK10939 182 tTGLLDLV-------TRDWDPALLEMAGL---RADILPP----VKETGTVLG-HVTAKAAAETGLRAGTPVVMGGGDVQL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 152 GGLGVigadvrghGLTCEGQpvtsrLAVICGT------------SSCHMGISKDPvfvpgvwgpyysAMVPGFWLNEGGQ 219
Cdd:PRK10939 247 GCLGL--------GVVRPGQ-----TAVLGGTfwqqvvnlpapvTDPNMNIRINP------------HVIPGMVQAESIS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 220 SVTGkLIdhMVQGHPAF-PELQAKATARCQSIYAYLNshldliKKAQ--PVGFLTVdLHVWPD-------FHGNRSPLad 289
Cdd:PRK10939 302 FFTG-LT--MRWFRDAFcAEEKLLAERLGIDAYSLLE------EMASrvPVGSHGI-IPIFSDvmrfkswYHAAPSFI-- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 290 ltlkgmvtGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQ 368
Cdd:PRK10939 370 --------NLSIDPEKCNKATLFRALEENAAIVSACNLQQIAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPV 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568929917 369 EVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQVFLRMVEHQ 429
Cdd:PRK10939 442 VKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENHELYQEAKEKWQAVYADQ 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
253-414 |
8.98e-09 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 57.40 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 253 YLNSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFI 326
Cdd:PLN02295 320 WLRDNLGIIKSASEIEALaaTVDdtggVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIA---RAVLESMCFQVKDV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 327 IETM------EAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSK 400
Cdd:PLN02295 397 LDAMrkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEKWK 476
|
170
....*....|....*...
gi 568929917 401 VGKVVFP----EHADKKY 414
Cdd:PLN02295 477 NTTTFRPkldeEERAKRY 494
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
319-394 |
1.75e-07 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 53.30 E-value: 1.75e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568929917 319 IAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAILGACASGDFTSVQEA 394
Cdd:cd07771 378 LALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEEG 453
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
248-380 |
1.96e-07 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 52.99 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 248 QSIYAYLNShLDLIKKAQPvgfLTVDlhvwPDFHGNRSplaDLTLKGMVTGLTLsqdlDDLAI--LYLATVQAIAFGTRF 325
Cdd:cd07777 315 DEIWEKLDE-LAESEESSD---LSVD----PTFFGERH---DPEGRGSITNIGE----SNFTLgnLFRALCRGIAENLHE 379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568929917 326 IIETMEAAGHSLSTLFLCGG-LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAIL 380
Cdd:cd07777 380 MLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALL 435
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
38-380 |
1.55e-06 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 49.95 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 38 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledlidd 106
Cdd:cd07772 129 LYWLKREKPEL-FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL--------- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 107 nyskignlvLLPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAgglgvigadvrghgltcegqpvtSRLAvicgtssc 186
Cdd:cd07772 199 ---------RKAWEVLGP-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP-------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 187 HMGISKDPvFV---PGVWgpyYSAMVPGFWLNEGGQSVTGKLIDHM-VQGHPA----FP-----ELQAKataRCQSIYAY 253
Cdd:cd07772 238 YLAAGKEP-FTllsTGTW---CIAMNPGNDLPLTELDLARDCLYNLdVFGRPVktarFMggreyERLVE---RIAKSFPQ 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 254 LNSHLDLIKkaqpvgFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAfgtrfiietMEAA 333
Cdd:cd07772 311 LPSLADLAK------LLARGTFALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYA---------LDLL 375
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 568929917 334 GHSLSTLFLCGGLSKNPLFVQMHADI-TGMPVVLSQEVESVLVGAAIL 380
Cdd:cd07772 376 GSGVGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
2-155 |
2.75e-06 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 48.49 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 2 WLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVtarslcsLV 79
Cdd:pfam00370 98 WKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKIHKFLTIHDYLRWRLTGV-------FV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 80 CKWTYSAEKG--------WDDSFWKMIGLEDlidDNYSKignlvLLPGAALGIGLTPEAARELGLPSGIAVAASLIDAHA 151
Cdd:pfam00370 170 TDHTNASRSMmfnihkldWDPELLAALGIPR---DHLPP-----LVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQA 241
|
....
gi 568929917 152 GGLG 155
Cdd:pfam00370 242 AAFG 245
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
334-417 |
6.26e-04 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 42.16 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929917 334 GHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKV----GKVVFPEH 409
Cdd:cd07776 423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502
|
....*...
gi 568929917 410 ADKKYYDK 417
Cdd:cd07776 503 EAAEVYDK 510
|
|
| |
