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Conserved domains on  [gi|500207396|ref|WP_011877617|]
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alpha-hydroxy-acid oxidizing protein [Desulforamulus reducens]

Protein Classification

alpha-hydroxy-acid oxidizing protein( domain architecture ID 10120247)

FMN-dependent alpha-hydroxyacid oxidizing protein such as bacterial lactate dehydrogenase and eukaryotic 2-hydroxy-acid oxidase

CATH:  3.20.20.70
EC:  1.-.-.-
Gene Ontology:  GO:0010181|GO:0016491
PubMed:  12206759|11257493

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 17-333 8.26e-99

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


:

Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 293.97  E-value: 8.26e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  17 YCRVCPVCDGRACSGEVPGMGGTGTGVSFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAPMTGTP-YNM 95
Cdd:cd02809    1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGlAHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  96 GGSLSEKEfismivsGSKQAGTLG--WTGDGADPEMYNSGLEAITNEQGYgipiiKPREQNVIIECIGRAERAGAKAVGV 173
Cdd:cd02809   81 DGELATAR-------AAAAAGIPFtlSTVSTTSLEEVAAAAPGPRWFQLY-----VPRDREITEDLLRRAEAAGYKALVL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 174 DIDGAGLVTMalkgqpvgpKSKREIKELVNATKLPFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILDFTPGAADVLPA 253
Cdd:cd02809  149 TVDTPVLGRR---------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPE 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 254 IAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVKFLIEKMTSELKQAMILTGCNTIKEIND 333
Cdd:cd02809  220 IVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
 
Name Accession Description Interval E-value
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 17-333 8.26e-99

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 293.97  E-value: 8.26e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  17 YCRVCPVCDGRACSGEVPGMGGTGTGVSFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAPMTGTP-YNM 95
Cdd:cd02809    1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGlAHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  96 GGSLSEKEfismivsGSKQAGTLG--WTGDGADPEMYNSGLEAITNEQGYgipiiKPREQNVIIECIGRAERAGAKAVGV 173
Cdd:cd02809   81 DGELATAR-------AAAAAGIPFtlSTVSTTSLEEVAAAAPGPRWFQLY-----VPRDREITEDLLRRAEAAGYKALVL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 174 DIDGAGLVTMalkgqpvgpKSKREIKELVNATKLPFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILDFTPGAADVLPA 253
Cdd:cd02809  149 TVDTPVLGRR---------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPE 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 254 IAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVKFLIEKMTSELKQAMILTGCNTIKEIND 333
Cdd:cd02809  220 IVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
FMN_dh pfam01070
FMN-dependent dehydrogenase;
37-337 2.14e-88

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 269.02  E-value: 2.14e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396   37 GGTGTGVSFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAPMTGTpyNMGGSLSEKefisMIVSGSKQAG 116
Cdd:pfam01070  15 GGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQ--GLAHPDGEL----ALARAAAAAG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  117 TLGWTgdgadPEMYNSGLEAITNE-------QGYgipiiKPREQNVIIECIGRAERAGAKAVGVDIDGAGL--------- 180
Cdd:pfam01070  89 IPFVL-----STVSSTSLEEVAAAaggplwfQLY-----VPRDRELTEDLLERAEAAGYKALVLTVDTPVLgrrerdlrn 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  181 -----------VTMALKGQPVGPKSK-----------------------REIKELVNATKLPFILKGIMTVDEAEMAVEA 226
Cdd:pfam01070 159 gftlpprltprNLLDLALHPRWALGVlrrggaggaaafvgsqfdpaltwDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  227 GVSAIVVSNHGGRILDFTPGAADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVK 306
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVA 318

                         330       340       350
                  ....*....|....*....|....*....|.
gi 500207396  307 FLIEKMTSELKQAMILTGCNTIKEINDSVIY 337
Cdd:pfam01070 319 HALEILRDELERTMALLGCKSIADLTPSLLR 349
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 37-337 8.01e-69

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 219.23  E-value: 8.01e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  37 GGTGTGVSFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAPMTGTpyNMGGSLSEK-------EF-ISMI 108
Cdd:COG1304   28 GGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGG--GLAHPDGELalaraaaAAgIPMG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 109 VSGskQAGTlgwtgdgadpemynsGLEAItNEQGYGIPII---KPREQNVIIECIGRAERAGAKA--VGVD--------- 174
Cdd:COG1304  106 LST--QSTT---------------SLEEV-AAAAPAPLWFqlyVPKDRGFTDDLLRRAEAAGADAlvLTVDtpvlgrrer 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 175 -----------IDGAGLVTMALKGQPVGPKSKRE---------------IKELVNATKLPFILKGIMTVDEAEMAVEAGV 228
Cdd:COG1304  168 dlregfsqpprLTPRNLLEAATHPRWALGLASLAawldtnfdpsltwddIAWLRERWPGPLIVKGVLSPEDARRAVDAGV 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 229 SAIVVSNHGGRILDFTPGAADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVKFL 308
Cdd:COG1304  248 DGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAGVARV 327

                        330       340
                 ....*....|....*....|....*....
gi 500207396 309 IEKMTSELKQAMILTGCNTIKEINDSVIY 337
Cdd:COG1304  328 LELLRAELRRAMALTGCRSLAELRRALLV 356
lldD PRK11197
L-lactate dehydrogenase; Provisional
 208-332 1.72e-41

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 148.63  E-value: 1.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 208 PFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILDFTPGAADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGV 287
Cdd:PRK11197 247 PMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIALGADTV 326

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 500207396 288 LVGRPLVVGAFGGHTEGVKFLIEKMTSELKQAMILTGCNTIKEIN 332
Cdd:PRK11197 327 LLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEIT 371
IMP_DH_rel_2 TIGR01304
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ...
 198-293 1.10e-04

IMP dehydrogenase family protein; This model represents a family of proteins, often annotated as a putative IMP dehydrogenase, related to IMP dehydrogenase and GMP reductase. Most species with a member of this family belong to the high GC Gram-positive bacteria, and these also have the IMP dehydrogenase described by TIGRFAMs equivalog model TIGR01302. [Unknown function, General]


Pssm-ID: 273547 [Multi-domain]  Cd Length: 369  Bit Score: 43.67  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  198 IKELVNATKLPFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILDFTPGAADVLP-AIAAAVKGK-----------VTIL 265
Cdd:TIGR01304 180 LKEFIGELDVPVIAGGVNDYTTALHLMRTGAAGVIVGPGGANTTRLVLGIEVPMAtAIADVAAARrdyldetggryVHVI 259

                          90       100
                  ....*....|....*....|....*...
gi 500207396  266 ADGGVRTGVDVLKLLALGADGVLVGRPL 293
Cdd:TIGR01304 260 ADGGIETSGDLVKAIACGADAVVLGSPL 287
 
Name Accession Description Interval E-value
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 17-333 8.26e-99

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 293.97  E-value: 8.26e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  17 YCRVCPVCDGRACSGEVPGMGGTGTGVSFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAPMTGTP-YNM 95
Cdd:cd02809    1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGlAHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  96 GGSLSEKEfismivsGSKQAGTLG--WTGDGADPEMYNSGLEAITNEQGYgipiiKPREQNVIIECIGRAERAGAKAVGV 173
Cdd:cd02809   81 DGELATAR-------AAAAAGIPFtlSTVSTTSLEEVAAAAPGPRWFQLY-----VPRDREITEDLLRRAEAAGYKALVL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 174 DIDGAGLVTMalkgqpvgpKSKREIKELVNATKLPFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILDFTPGAADVLPA 253
Cdd:cd02809  149 TVDTPVLGRR---------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPE 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 254 IAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVKFLIEKMTSELKQAMILTGCNTIKEIND 333
Cdd:cd02809  220 IVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
FMN_dh pfam01070
FMN-dependent dehydrogenase;
37-337 2.14e-88

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 269.02  E-value: 2.14e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396   37 GGTGTGVSFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAPMTGTpyNMGGSLSEKefisMIVSGSKQAG 116
Cdd:pfam01070  15 GGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQ--GLAHPDGEL----ALARAAAAAG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  117 TLGWTgdgadPEMYNSGLEAITNE-------QGYgipiiKPREQNVIIECIGRAERAGAKAVGVDIDGAGL--------- 180
Cdd:pfam01070  89 IPFVL-----STVSSTSLEEVAAAaggplwfQLY-----VPRDRELTEDLLERAEAAGYKALVLTVDTPVLgrrerdlrn 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  181 -----------VTMALKGQPVGPKSK-----------------------REIKELVNATKLPFILKGIMTVDEAEMAVEA 226
Cdd:pfam01070 159 gftlpprltprNLLDLALHPRWALGVlrrggaggaaafvgsqfdpaltwDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  227 GVSAIVVSNHGGRILDFTPGAADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVK 306
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVA 318

                         330       340       350
                  ....*....|....*....|....*....|.
gi 500207396  307 FLIEKMTSELKQAMILTGCNTIKEINDSVIY 337
Cdd:pfam01070 319 HALEILRDELERTMALLGCKSIADLTPSLLR 349
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 37-337 8.01e-69

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 219.23  E-value: 8.01e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  37 GGTGTGVSFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAPMTGTpyNMGGSLSEK-------EF-ISMI 108
Cdd:COG1304   28 GGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGG--GLAHPDGELalaraaaAAgIPMG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 109 VSGskQAGTlgwtgdgadpemynsGLEAItNEQGYGIPII---KPREQNVIIECIGRAERAGAKA--VGVD--------- 174
Cdd:COG1304  106 LST--QSTT---------------SLEEV-AAAAPAPLWFqlyVPKDRGFTDDLLRRAEAAGADAlvLTVDtpvlgrrer 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 175 -----------IDGAGLVTMALKGQPVGPKSKRE---------------IKELVNATKLPFILKGIMTVDEAEMAVEAGV 228
Cdd:COG1304  168 dlregfsqpprLTPRNLLEAATHPRWALGLASLAawldtnfdpsltwddIAWLRERWPGPLIVKGVLSPEDARRAVDAGV 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 229 SAIVVSNHGGRILDFTPGAADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVKFL 308
Cdd:COG1304  248 DGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAGVARV 327

                        330       340
                 ....*....|....*....|....*....
gi 500207396 309 IEKMTSELKQAMILTGCNTIKEINDSVIY 337
Cdd:COG1304  328 LELLRAELRRAMALTGCRSLAELRRALLV 356
LMO_FMN cd03332
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ...
 37-336 8.38e-52

L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.


Pssm-ID: 239448 [Multi-domain]  Cd Length: 383  Bit Score: 175.93  E-value: 8.38e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  37 GGTGTGVSFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAPMtgtpynmgGSLSekefismIVSGSKQAG 116
Cdd:cd03332   42 GGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPI--------GVQE-------LFHPDAELA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 117 TLGWTGDGADPEMY----NSGLEAITNEQGYG---IPIIKPREQNVIIECIGRAERAGAKAVGVDID------------- 176
Cdd:cd03332  107 TARAAAELGVPYILstasSSSIEDVAAAAGDAprwFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDtwslgwrprdldl 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 177 -------GAGL-------VTMALKGQPVGPKSKR-----------------------EIKELVNATKLPFILKGIMTVDE 219
Cdd:cd03332  187 gylpflrGIGIanyfsdpVFRKKLAEPVGEDPEApppmeaavarfvsvfsgpsltweDLAFLREWTDLPIVLKGILHPDD 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 220 AEMAVEAGVSAIVVSNHGGRILDFTPGAADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVG-AF 298
Cdd:cd03332  267 ARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGRPYAYGlAL 346

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 500207396 299 GGhTEGVKFLIEKMTSELKQAMILTGCNTIKEINDSVI 336
Cdd:cd03332  347 GG-EDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 37-331 1.37e-50

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088 [Multi-domain]  Cd Length: 351  Bit Score: 171.86  E-value: 1.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  37 GGTGTGVSFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAPMTGtpynMGGSLSEKEFISmiVSGSKQAG 116
Cdd:cd04737   29 GGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAA----HGLAHATGEVAT--ARGMAEVG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 117 TLgWTGDGADpemyNSGLEAITNEQGYG-----IPIIKPREQNVIIecIGRAERAGAKAVGVDID--------------- 176
Cdd:cd04737  103 SL-FSISTYS----NTSLEEIAKASNGGpkwfqLYMSKDDGFNRSL--LDRAKAAGAKAIILTADatvggnreadirnkf 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 177 ----GAGLVTMALKGQPVGPK------------SKREIKELVNATKLPFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRI 240
Cdd:cd04737  176 qfpfGMPNLNHFSEGTGKGKGiseiyaaakqklSPADIEFIAKISGLPVIVKGIQSPEDADVAINAGADGIWVSNHGGRQ 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 241 LDFTPGAADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVKFLIEKMTSELKQAM 320
Cdd:cd04737  256 LDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGVASVLEHLNKELKIVM 335

                        330
                 ....*....|.
gi 500207396 321 ILTGCNTIKEI 331
Cdd:cd04737  336 QLAGTRTIEDV 346
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
 38-332 3.75e-49

Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.


Pssm-ID: 239238 [Multi-domain]  Cd Length: 344  Bit Score: 167.77  E-value: 3.75e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  38 GTGTGVSFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAPMTGTPYnmGGSLSEKEfismIVSGSKQAGT 117
Cdd:cd02922   22 GADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKL--AHPDGELN----LARAAGKHGI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 118 LGWTGDGAD---PEMYnsglEAITNEQGYGIPIIKPREQNVIIECIGRAERAGAKAVGVDIDGAGL----------VTMA 184
Cdd:cd02922   96 LQMISTNAScslEEIV----DARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLgkrerderlkAEEA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 185 LKGQPVGPKSKRE--------------------IKELVNATKLPFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILDFT 244
Cdd:cd02922  172 VSDGPAGKKTKAKgggagramsgfidptltwddIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTA 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 245 PGAADVLPAI---AAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVKFLIEKMTSELKQAMI 321
Cdd:cd02922  252 PAPIEVLLEIrkhCPEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMR 331

                        330
                 ....*....|.
gi 500207396 322 LTGCNTIKEIN 332
Cdd:cd02922  332 LLGVTSLDQLG 342
lldD PRK11197
L-lactate dehydrogenase; Provisional
 208-332 1.72e-41

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 148.63  E-value: 1.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 208 PFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILDFTPGAADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGV 287
Cdd:PRK11197 247 PMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIALGADTV 326

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 500207396 288 LVGRPLVVGAFGGHTEGVKFLIEKMTSELKQAMILTGCNTIKEIN 332
Cdd:PRK11197 327 LLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEIT 371
PLN02535 PLN02535
glycolate oxidase
 37-334 9.20e-39

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 141.13  E-value: 9.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  37 GGTGTGVSFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAP--MTGTPYNMGGSLSEKEFIS----MIVS 110
Cdd:PLN02535  29 GGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPtaMHKLAHPEGEIATARAAAAcntiMVLS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 111 GSKQAGTlgwtgdgadpEMYNSGLEAITNEQGYgipIIKPREQNVIIecIGRAERAGAKAV--GVDIDGAGLVTMALKGQ 188
Cdd:PLN02535 109 FMASCTV----------EEVASSCNAVRFLQLY---VYKRRDIAAQL--VQRAEKNGYKAIvlTADVPRLGRREADIKNK 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 189 PVGPKSK--------------------------------REIKELVNATKLPFILKGIMTVDEAEMAVEAGVSAIVVSNH 236
Cdd:PLN02535 174 MISPQLKnfegllstevvsdkgsgleafasetfdaslswKDIEWLRSITNLPILIKGVLTREDAIKAVEVGVAGIIVSNH 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 237 GGRILDFTPGAADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVKFLIEKMTSEL 316
Cdd:PLN02535 254 GARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGEDGVRKVIEMLKDEL 333

                        330
                 ....*....|....*...
gi 500207396 317 KQAMILTGCNTIKEINDS 334
Cdd:PLN02535 334 EITMALSGCPSVKDITRS 351
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
 44-331 2.98e-33

probable peroxisomal (S)-2-hydroxy-acid oxidase


Pssm-ID: 166134 [Multi-domain]  Cd Length: 367  Bit Score: 126.38  E-value: 2.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  44 SFRNNLNALASYNLNMRTLHNAKNPSTETELFGVALTSPIMAAPmtgTPYNmggSLSEKEFISMIVSGSKQAGTLGWTGD 123
Cdd:PLN02493  34 TLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAP---TAMQ---KMAHPDGEYATARAASAAGTIMTLSS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 124 GAdpemyNSGLEAITNeQGYGIPIIKP---REQNVIIECIGRAERAGAKAVGVDID------------------------ 176
Cdd:PLN02493 108 WA-----TSSVEEVAS-TGPGIRFFQLyvyKNRNVVEQLVRRAERAGFKAIALTVDtprlgrresdiknrftlppnltlk 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 177 --------------GAGLVTMaLKGQPVGPKSKREIKELVNATKLPFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILD 242
Cdd:PLN02493 182 nfegldlgkmdeanDSGLASY-VAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLD 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 243 FTPGAADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVKFLIEKMTSELKQAMIL 322
Cdd:PLN02493 261 YVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMAL 340


                 ....*....
gi 500207396 323 TGCNTIKEI 331
Cdd:PLN02493 341 SGCRSLKEI 349
PLN02979 PLN02979
glycolate oxidase
 60-332 1.46e-32

glycolate oxidase


Pssm-ID: 166620  Cd Length: 366  Bit Score: 124.45  E-value: 1.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  60 RTLHNAKNPSTETELFGVALTSPIMAAPMTGTpynmggSLSEKEFISMIVSGSKQAGTLGWTGDGAdpemyNSGLEAITN 139
Cdd:PLN02979  49 RILIDVSKIDMTTTVLGFKISMPIMVAPTAMQ------KMAHPDGEYATARAASAAGTIMTLSSWA-----TSSVEEVAS 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 140 eQGYGIPIIKP---REQNVIIECIGRAERAGAKAVGVDID--------------------------------------GA 178
Cdd:PLN02979 118 -TGPGIRFFQLyvyKNRNVVEQLVRRAERAGFKAIALTVDtprlgrresdiknrftlppnltlknfegldlgkmdeanDS 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 179 GLVTMaLKGQPVGPKSKREIKELVNATKLPFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILDFTPGAADVLPAIAAAV 258
Cdd:PLN02979 197 GLASY-VAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKAT 275

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500207396 259 KGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVKFLIEKMTSELKQAMILTGCNTIKEIN 332
Cdd:PLN02979 276 QGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEIS 349
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
 210-332 7.12e-24

Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240087  Cd Length: 361  Bit Score: 100.29  E-value: 7.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 210 ILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILDFTPGAADVLPAIAAAVKGKVTIlaDGGVRTGVDVLKLLALGADGVLV 289
Cdd:cd04736  240 LVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYKPVLI--DSGIRRGSDIVKALALGANAVLL 317

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 500207396 290 GRPLVVGAFGGHTEGVKFLIEKMTSELKQAMILTGCNTIKEIN 332
Cdd:cd04736  318 GRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLT 360
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 198-330 3.17e-18

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


Pssm-ID: 239205 [Multi-domain]  Cd Length: 326  Bit Score: 84.09  E-value: 3.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 198 IKELVNATKLPFILKGI---MTVDEAEMAVEAGVSAIVVSNHGG----------------RILDF-----TPGAADVLPA 253
Cdd:cd02811  170 IEELVKALSVPVIVKEVgfgISRETAKRLADAGVKAIDVAGAGGtswarvenyrakdsdqRLAEYfadwgIPTAASLLEV 249

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500207396 254 IAAAvkGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGhTEGVKFLIEKMTSELKQAMILTGCNTIKE 330
Cdd:cd02811  250 RSAL--PDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKAALEG-EEAVIETIEQIIEELRTAMFLTGAKNLAE 323
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 83-291 8.01e-13

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 66.46  E-value: 8.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  83 IMAAPMTGTPYNMGGSLSEKEFISmivsgskQAGTLGWTGDGADPEMYNSGLEAITNEQ--GYGIPIIKpreQNVIIECI 160
Cdd:cd04722    1 VILALLAGGPSGDPVELAKAAAEA-------GADAIIVGTRSSDPEEAETDDKEVLKEVaaETDLPLGV---QLAINDAA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 161 GRAERAGAKAV-----GVDIDGAGLVTMALkgqpvGPKSKREIKELVNatKLPFILKGIMTVDEAEM-AVEAGVSAIVVS 234
Cdd:cd04722   71 AAVDIAAAAARaagadGVEIHGAVGYLARE-----DLELIRELREAVP--DVKVVVKLSPTGELAAAaAEEAGVDEVGLG 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 500207396 235 NHGGRILDFTPGAADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGR 291
Cdd:cd04722  144 NGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 216-290 2.68e-10

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 59.80  E-value: 2.68e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500207396 216 TVDEAEMAVEAGVSAIVVSNH--GGRILDFTPGAADVLPAIAAAVKgkVTILADGGVRTGVDVLKLLALGADGVLVG 290
Cdd:cd04730  111 SVEEARKAEAAGADALVAQGAeaGGHRGTFDIGTFALVPEVRDAVD--IPVIAAGGIADGRGIAAALALGADGVQMG 185
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 216-290 3.06e-09

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 57.43  E-value: 3.06e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500207396 216 TVDEAEMAVEAGVSAIVVSNH--GGRILDFTPGAADVLPAIAAAVKgkVTILADGGVRTGVDVLKLLALGADGVLVG 290
Cdd:COG2070  113 SVREARKAEKAGADAVVAEGAeaGGHRGADEVSTFALVPEVRDAVD--IPVIAAGGIADGRGIAAALALGADGVQMG 187
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 195-310 1.03e-07

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 52.90  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 195 KREIKELVNatKLPFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRIlDFT--------PGAADVLPAIAAAVKGKVTILA 266
Cdd:cd00381  126 IKFIKKKYP--NVDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSI-CTTrivtgvgvPQATAVADVAAAARDYGVPVIA 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 500207396 267 DGGVRTGVDVLKLLALGADGVLVGRPlvvgaFGGHTE--GVKFLIE 310
Cdd:cd00381  203 DGGIRTSGDIVKALAAGADAVMLGSL-----LAGTDEspGEYIEIN 243
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 198-299 1.23e-07

Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 51.73  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 198 IKELVNATKLPFILK-------GIMTVDEAEMAVEAGVSAIVVsnHGGRILDFTPGAADvLPAIAAAVKG-KVTILADGG 269
Cdd:cd02801  115 VRAVREAVPIPVTVKirlgwddEEETLELAKALEDAGASALTV--HGRTREQRYSGPAD-WDYIAEIKEAvSIPVIANGD 191

                         90       100       110
                 ....*....|....*....|....*....|.
gi 500207396 270 VRTGVDVLKLLAL-GADGVLVGRplvvGAFG 299
Cdd:cd02801  192 IFSLEDALRCLEQtGVDGVMIGR----GALG 218
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 198-299 5.55e-07

tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 50.48  E-value: 5.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 198 IKELVNATKLPFILK---GI-----MTVDEAEMAVEAGVSAIVVsnHGgRI-LDFTPGAADvLPAIAAAVKG-KVTILAD 267
Cdd:COG0042  122 VKAVVEAVDVPVTVKirlGWddddeNALEFARIAEDAGAAALTV--HG-RTrEQRYKGPAD-WDAIARVKEAvSIPVIGN 197

                         90       100       110
                 ....*....|....*....|....*....|...
gi 500207396 268 GGVRTGVDVLKLLAL-GADGVLVGRplvvGAFG 299
Cdd:COG0042  198 GDIFSPEDAKRMLEEtGCDGVMIGR----GALG 226
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
 217-291 5.94e-07

Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.


Pssm-ID: 239202 [Multi-domain]  Cd Length: 392  Bit Score: 50.62  E-value: 5.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 217 VDEAEMAVEAG-VSAIVVSNHGG-------RILDFT--PgaadVLPAIAAAV--------KGKVTILADGGVRTGVDVLK 278
Cdd:cd02808  227 EGDIAAGVAAAgADFITIDGAEGgtgaaplTFIDHVglP----TELGLARAHqalvknglRDRVSLIASGGLRTGADVAK 302

                         90
                 ....*....|...
gi 500207396 279 LLALGADGVLVGR 291
Cdd:cd02808  303 ALALGADAVGIGT 315
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
 223-295 5.57e-06

Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.


Pssm-ID: 396287 [Multi-domain]  Cd Length: 367  Bit Score: 47.71  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  223 AVEAGVSAIVVSNHGGrildfTPGAADV-------LP---AIAAAVKG--------KVTILADGGVRTGVDVLKLLALGA 284
Cdd:pfam01645 222 VAKAGADIILIDGYDG-----GTGASPKtsikhagLPwelALAEAHQTlkenglrdRVSLIADGGLRTGADVAKAAALGA 296

                          90
                  ....*....|.
gi 500207396  285 DGVLVGRPLVV 295
Cdd:pfam01645 297 DAVYIGTAALI 307
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 156-290 5.81e-06

Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239204 [Multi-domain]  Cd Length: 289  Bit Score: 47.35  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 156 IIECIGRAERAGAKAVGVDIDGAGLVTMALKGQpvGPKSKREI-KELVNATKLPFILKGIMTVDEAEM------AVEAGV 228
Cdd:cd02810  113 YVELARKIERAGAKALELNLSCPNVGGGRQLGQ--DPEAVANLlKAVKAAVDIPLLVKLSPYFDLEDIvelakaAERAGA 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 229 SAIVVSN--HGGRILDFTPGA-----------ADVLPA-------IAAAVKGKVTILADGGVRTGVDVLKLLALGADGVL 288
Cdd:cd02810  191 DGLTAINtiSGRVVDLKTVGPgpkrgtgglsgAPIRPLalrwvarLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQ 270


                 ..
gi 500207396 289 VG 290
Cdd:cd02810  271 VA 272
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 131-328 8.79e-06

Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439937 [Multi-domain]  Cd Length: 296  Bit Score: 46.60  E-value: 8.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 131 NSGLEAITNE----QGYGIPII----KpreqNVI---IECIGRAERAGAKAVGVDI-----DGAGlvtMALkGQpvGPKS 194
Cdd:COG0167   75 NPGVDAFLERllpaKRYDVPVIvnigG----NTVedyVELARRLADAGADYLELNIscpntPGGG---RAL-GQ--DPEA 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 195 KREI-KELVNATKLPFILKgiMT------VDEAEMAVEAGVSAIVVSN----------HGGRILDFTPG----------A 247
Cdd:COG0167  145 LAELlAAVKAATDKPVLVK--LApdltdiVEIARAAEEAGADGVIAINttlgraidleTRRPVLANEAGglsgpalkpiA 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 248 ADVLPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGghtegvkfLIEKMTSELKQAMILTGCNT 327
Cdd:COG0167  223 LRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPG--------LVRRIIRGLEAYLEEKGFSS 294


                 .
gi 500207396 328 I 328
Cdd:COG0167  295 I 295
IMP_DH_rel_2 TIGR01304
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ...
 198-293 1.10e-04

IMP dehydrogenase family protein; This model represents a family of proteins, often annotated as a putative IMP dehydrogenase, related to IMP dehydrogenase and GMP reductase. Most species with a member of this family belong to the high GC Gram-positive bacteria, and these also have the IMP dehydrogenase described by TIGRFAMs equivalog model TIGR01302. [Unknown function, General]


Pssm-ID: 273547 [Multi-domain]  Cd Length: 369  Bit Score: 43.67  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  198 IKELVNATKLPFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILDFTPGAADVLP-AIAAAVKGK-----------VTIL 265
Cdd:TIGR01304 180 LKEFIGELDVPVIAGGVNDYTTALHLMRTGAAGVIVGPGGANTTRLVLGIEVPMAtAIADVAAARrdyldetggryVHVI 259

                          90       100
                  ....*....|....*....|....*...
gi 500207396  266 ADGGVRTGVDVLKLLALGADGVLVGRPL 293
Cdd:TIGR01304 260 ADGGIETSGDLVKAIACGADAVVLGSPL 287
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 198-291 1.49e-04

Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.


Pssm-ID: 426126  Cd Length: 309  Bit Score: 43.08  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  198 IKELVNATKLPFILK---GI-----MTVDEAEMAVEAGVSAIVVsnHGGRILDFTPGAADvLPAIAAaVKGKVTI--LAD 267
Cdd:pfam01207 114 VKAVVKAVGIPVTVKiriGWddsheNAVEIAKIVEDAGAQALTV--HGRTRAQNYEGTAD-WDAIKQ-VKQAVSIpvIAN 189

                          90       100
                  ....*....|....*....|....*
gi 500207396  268 GGVRTGVDVLKLLA-LGADGVLVGR 291
Cdd:pfam01207 190 GDITDPEDAQRCLAyTGADGVMIGR 214
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 211-294 2.00e-04

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 42.56  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 211 LKGIMTVDE----AEMAVEAGVSAIVVS----NHGGRILDFTPGAADVLPAIAAAVKGKVTI--LADGGVRTGVDVLKLL 280
Cdd:cd02803  221 VPGGLTLEEaieiAKALEEAGVDALHVSggsyESPPPIIPPPYVPEGYFLELAEKIKKAVKIpvIAVGGIRDPEVAEEIL 300

                         90
                 ....*....|....*
gi 500207396 281 ALG-ADGVLVGRPLV 294
Cdd:cd02803  301 AEGkADLVALGRALL 315
PRK06843 PRK06843
inosine 5-monophosphate dehydrogenase; Validated
 165-297 2.08e-04

inosine 5-monophosphate dehydrogenase; Validated


Pssm-ID: 180725 [Multi-domain]  Cd Length: 404  Bit Score: 42.72  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 165 RAGAkAVGVDIDGAGLVTMALKGQ-------PVGPKSKReIKELVNATK-----LPFILKGIMTVDEAEMAVEAGVSAIV 232
Cdd:PRK06843 143 RVGA-AVSIDIDTIERVEELVKAHvdilvidSAHGHSTR-IIELVKKIKtkypnLDLIAGNIVTKEAALDLISVGADCLK 220

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500207396 233 VSNHGGRILDFTPGAADVLPAIAAAV-------KGKVTILADGGVRTGVDVLKLLALGADGVLVGRpLVVGA 297
Cdd:PRK06843 221 VGIGPGSICTTRIVAGVGVPQITAICdvyevckNTNICIIADGGIRFSGDVVKAIAAGADSVMIGN-LFAGT 291
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
 162-290 2.85e-04

Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.


Pssm-ID: 188634 [Multi-domain]  Cd Length: 201  Bit Score: 41.54  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 162 RAERAGAKAVGVDIDgaglVTMALKGQPvgPKSKREIKELVNATKLPFILKGIM----------TVDEAEMAVEAGVSAI 231
Cdd:cd00945   73 EAIDLGADEIDVVIN----IGSLKEGDW--EEVLEEIAAVVEAADGGLPLKVILetrglktadeIAKAARIAAEAGADFI 146

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500207396 232 VVSnhggriLDFTPGAADV--LPAIAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVG 290
Cdd:cd00945  147 KTS------TGFGGGGATVedVKLMKEAVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 216-294 2.92e-04

Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.


Pssm-ID: 238203  Cd Length: 217  Bit Score: 41.68  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 216 TVDEAEMAVEAGVSAIVVSNhggRIL-DFT--PGAADVLpaiAAAVKGKVTILADGGVRTGVDVLKLLALGADGVLVGRP 292
Cdd:cd00331  130 DEEELERALALGAKIIGINN---RDLkTFEvdLNTTERL---APLIPKDVILVSESGISTPEDVKRLAEAGADAVLIGES 203


                 ..
gi 500207396 293 LV 294
Cdd:cd00331  204 LM 205
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ...
 258-295 3.51e-04

Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 439839  Cd Length: 728  Bit Score: 42.54  E-value: 3.51e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 500207396 258 VKGKVTILADGGVRTGVDVLKLLALGADGVLVGR-PLVV 295
Cdd:COG0069  437 LRDRIRLIADGKLKTGRDVAIAAALGADEFGFARaFMVA 475
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 198-293 4.84e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 41.88  E-value: 4.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 198 IKELVNAT-KLPFILKGIMTVDEAEMAVEAGVSAIVVSNHGGRILdFTPGAADVLPAIAAAV--------KGKVTILADG 268
Cdd:PTZ00314 273 IKKLKSNYpHVDIIAGNVVTADQAKNLIDAGADGLRIGMGSGSIC-ITQEVCAVGRPQASAVyhvaryarERGVPCIADG 351

                         90       100
                 ....*....|....*....|....*
gi 500207396 269 GVRTGVDVLKLLALGADGVLVGRPL 293
Cdd:PTZ00314 352 GIKNSGDICKALALGADCVMLGSLL 376
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 209-290 7.95e-04

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 40.96  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396  209 FILKGIMTVDEAEMAVEAGVSAIVV--SNHGGRILDFTPGAAD---VLPAIAAAVKgkVTILADGGVRTGVDVLKLLALG 283
Cdd:pfam03060 138 ALIPTISSAKEARIAEARGADALIVqgPEAGGHQGTPEYGDKGlfrLVPQVPDAVD--IPVIAAGGIWDRRGVAAALALG 215


                  ....*..
gi 500207396  284 ADGVLVG 290
Cdd:pfam03060 216 ASGVQMG 222
DeoC cd00959
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
 196-285 9.89e-04

2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family. DERA belongs to the class I aldolases and catalyzes a reversible aldol reaction between acetaldehyde and glyceraldehyde 3-phosphate to generate 2-deoxyribose 5-phosphate. DERA is unique in catalyzing the aldol reaction between two aldehydes, and its broad substrate specificity confers considerable utility as a biocatalyst, offering an environmentally benign alternative to chiral transition metal catalysis of the asymmetric aldol reaction.


Pssm-ID: 188646  Cd Length: 203  Bit Score: 39.82  E-value: 9.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 196 REIKELVNATKlPFILKGI-----MTVDE----AEMAVEAGVSAIVVSNhgGrildFTPGAA---DVLpAIAAAVKGKVT 263
Cdd:cd00959  105 EEIAAVVEACG-GAPLKVIletglLTDEEiikaCEIAIEAGADFIKTST--G----FGPGGAtveDVK-LMKEAVGGRVG 176

                         90       100
                 ....*....|....*....|..
gi 500207396 264 ILADGGVRTGVDVLKLLALGAD 285
Cdd:cd00959  177 VKAAGGIRTLEDALAMIEAGAT 198
DeoC COG0274
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
195-285 1.17e-03

Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];


Pssm-ID: 440043  Cd Length: 219  Bit Score: 39.66  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 195 KREIKELVNATKlPFILKGI-----MTVDE----AEMAVEAGVsaivvsnhggrilDF--------TPGA--ADVLpAIA 255
Cdd:COG0274  106 EEEIAAVVEAAG-GAVLKVIletglLTDEEirkaCELAIEAGA-------------DFvktstgfgPGGAtvEDVR-LMR 170

                         90       100       110
                 ....*....|....*....|....*....|
gi 500207396 256 AAVKGKVTILADGGVRTGVDVLKLLALGAD 285
Cdd:COG0274  171 ETVGGRVGVKASGGIRTLEDALAMIEAGAT 200
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 196-295 1.49e-03

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 39.89  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 196 REIKELVNA-TKLPFIL----------KGIMTVDEA----EMAVEAGVSAIVVSNHGGRILDFTPGAAD--VLPAIAAAV 258
Cdd:cd04735  202 KAVQEVIDKhADKDFILgyrfspeepeEPGIRMEDTlalvDKLADKGLDYLHISLWDFDRKSRRGRDDNqtIMELVKERI 281

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 500207396 259 KGKVTILADGGVRTGVDVLKLLALGADGVLVGRPLVV 295
Cdd:cd04735  282 AGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLV 318
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 164-298 1.84e-03

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 39.39  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 164 ERAGAKAVG-VDIDGAglvtmaLKGQPVgpkSKREIKELVNATKLPFILKG-IMTVDEAEMAVEAGVSAIVVS------- 234
Cdd:cd04732   39 EEAGAKWLHvVDLDGA------KGGEPV---NLELIEEIVKAVGIPVQVGGgIRSLEDIERLLDLGVSRVIIGtaavknp 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 235 --------NHGG-RI---LD----------------FTP----------GAA------------------DVLPAIAAAV 258
Cdd:cd04732  110 elvkellkEYGGeRIvvgLDakdgkvatkgwletseVSLeelakrfeelGVKaiiytdisrdgtlsgpnfELYKELAAAT 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 500207396 259 KGKVtiLADGGVRTGVDVLKLLALGADGVLVGRPLVVGAF 298
Cdd:cd04732  190 GIPV--IASGGVSSLDDIKALKELGVAGVIVGKALYEGKI 227
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 162-324 1.90e-03

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 39.11  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 162 RAERAGAKAVGVdidgaglVTMALKGQPVGPKSKREIKELVNATKLPFILKGIMT------VDEAEMAVEAGVSAIVVSN 235
Cdd:cd04722   20 AAAEAGADAIIV-------GTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINdaaaavDIAAAAARAAGADGVEIHG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 236 HGGRILDFTPGAADVLPAIAAAVKgkvtILADGGVRTGVDVLKLLALGADGVLVGRPLVVGAFGGHTEGVKFLIEKMTSE 315
Cdd:cd04722   93 AVGYLAREDLELIRELREAVPDVK----VVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRG 168


                 ....*....
gi 500207396 316 LKQAMILTG 324
Cdd:cd04722  169 SKVPVIAGG 177
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 164-298 5.26e-03

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 37.71  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 164 ERAGAKAVG-VDIDGAglvtmaLKGQPVgpkSKREIKELVNATKLPFILKG-IMTVDEAEMAVEAGVSAIVV-------- 233
Cdd:COG0106   39 EDAGAEWLHlVDLDGA------FAGKPV---NLELIEEIAKATGLPVQVGGgIRSLEDIERLLDAGASRVILgtaavkdp 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500207396 234 -------SNHGGRIL-------------------DFTP----------GAADVL------------P------AIAAAVK 259
Cdd:COG0106  110 elvkealEEFPERIVvgldardgkvatdgwqetsGVDLeelakrfedaGVAAILytdisrdgtlqgPnlelyrELAAATG 189

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 500207396 260 GKVTilADGGVRTGVDVLKLLALGADGVLVGRPLVVGAF 298
Cdd:COG0106  190 IPVI--ASGGVSSLDDLRALKELGVEGAIVGKALYEGKI 226
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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