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Conserved domains on  [gi|501109392|ref|WP_012159017|]
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alpha-hydroxy-acid oxidizing protein [Alkaliphilus oremlandii]

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
SCOP:  4000080

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 ...
 45-333 2.43e-94

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: 282.41  E-value: 2.43e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  45 FIRNWQKIQDVKINLDTIIEESPIDTSIELFGQKFTYPVFAAPIGAVGL-NYSPALDDFEYtkaiiggCKEAGvIGF--- 120
Cdd:cd02809   29 LRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLaHPDGELATARA-------AAAAG-IPFtls 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 121 TGDGVKDEfydlplQVVKENNGHG----IPTIKPWKKEEIIAKIKKAeenGAPAVAMDIDAAGLVTLallgkpvgtKSIE 196
Cdd:cd02809  101 TVSTTSLE------EVAAAAPGPRwfqlYVPRDREITEDLLRRAEAA---GYKALVLTVDTPVLGRR---------LTWD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 197 DLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADAVKGRMKIFVDGGFRTGLDI 276
Cdd:cd02809  163 DLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDV 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501109392 277 FKAIALGADAVLIGRPYAVAAYGGGAEGVKVYTEKIGNELKETMIMAGCHNLADIKR 333
Cdd:cd02809  243 LKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 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 ...
 45-333 2.43e-94

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: 282.41  E-value: 2.43e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  45 FIRNWQKIQDVKINLDTIIEESPIDTSIELFGQKFTYPVFAAPIGAVGL-NYSPALDDFEYtkaiiggCKEAGvIGF--- 120
Cdd:cd02809   29 LRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLaHPDGELATARA-------AAAAG-IPFtls 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 121 TGDGVKDEfydlplQVVKENNGHG----IPTIKPWKKEEIIAKIKKAeenGAPAVAMDIDAAGLVTLallgkpvgtKSIE 196
Cdd:cd02809  101 TVSTTSLE------EVAAAAPGPRwfqlYVPRDREITEDLLRRAEAA---GYKALVLTVDTPVLGRR---------LTWD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 197 DLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADAVKGRMKIFVDGGFRTGLDI 276
Cdd:cd02809  163 DLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDV 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501109392 277 FKAIALGADAVLIGRPYAVAAYGGGAEGVKVYTEKIGNELKETMIMAGCHNLADIKR 333
Cdd:cd02809  243 LKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
FMN_dh pfam01070
FMN-dependent dehydrogenase;
47-336 5.31e-88

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 267.86  E-value: 5.31e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392   47 RNWQKIQDVKINLDTIIEESPIDTSIELFGQKFTYPVFAAPIGAVGLnYSPALDdfeytKAIIGGCKEAGVI----GFTG 122
Cdd:pfam01070  25 RNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGL-AHPDGE-----LALARAAAAAGIPfvlsTVSS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  123 DGVKDefydlplqVVKENNGHGIPTIKPWKKEEIIAK-IKKAEENGAPAVAMDIDAAGL--------------------V 181
Cdd:pfam01070  99 TSLEE--------VAAAAGGPLWFQLYVPRDRELTEDlLERAEAAGYKALVLTVDTPVLgrrerdlrngftlpprltprN 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  182 TLALLGKPVGTKSI-----------------------EDLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGG 238
Cdd:pfam01070 171 LLDLALHPRWALGVlrrggaggaaafvgsqfdpaltwDDLAWLRERWKGPLVVKGILSPEDAKRAVEAGVDGIVVSNHGG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  239 RVLDHTPATIEVLPAIADAVKGRMKIFVDGGFRTGLDIFKAIALGADAVLIGRPYAVAAYGGGAEGVKVYTEKIGNELKE 318
Cdd:pfam01070 251 RQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAHALEILRDELER 330

                         330
                  ....*....|....*...
gi 501109392  319 TMIMAGCHNLADIKRDRV 336
Cdd:pfam01070 331 TMALLGCKSIADLTPSLL 348
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 66-338 1.08e-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: 221.16  E-value: 1.08e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  66 SPIDTSIELFGQKFTYPVFAAPIGAVGL----------------------------------NYSPA--------LDDFE 103
Cdd:COG1304   57 SEIDLSTTLLGKRLAAPFLIAPMGGGGLahpdgelalaraaaaagipmglstqsttsleevaAAAPAplwfqlyvPKDRG 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 104 YTKAIIGGCKEAG--VIGFTgdgvkdefYDLPLQVVKEN---NGHGIP-TIKPWKKEEIIAKIKKAEENGAPAVAMDIDA 177
Cdd:COG1304  137 FTDDLLRRAEAAGadALVLT--------VDTPVLGRRERdlrEGFSQPpRLTPRNLLEAATHPRWALGLASLAAWLDTNF 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 178 AGLVTLallgkpvgtksiEDLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADA 257
Cdd:COG1304  209 DPSLTW------------DDIAWLRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAA 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 258 VKGRMKIFVDGGFRTGLDIFKAIALGADAVLIGRPYAVAAYGGGAEGVKVYTEKIGNELKETMIMAGCHNLADIKRDRVF 337
Cdd:COG1304  277 VGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356


                 .
gi 501109392 338 L 338
Cdd:COG1304  357 L 357
lldD PRK11197
L-lactate dehydrogenase; Provisional
 47-334 8.02e-45

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 157.49  E-value: 8.02e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  47 RNWQKIQDVKINLDTIIEESPIDTSIELFGQKFTYPVFAAPIGAVGLN-------------------------------Y 95
Cdd:PRK11197  37 RNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGMYarrgevqaaraadakgipftlstvsvcpieeV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  96 SPA-----------LDDFEYTKAIIGGCKEAGV--IGFTgdgvkdefYDLPLQVVKENNGH-GIPTIKPWKKEEIIAKIK 161
Cdd:PRK11197 117 APAikrpmwfqlyvLRDRGFMRNALERAKAAGCstLVFT--------VDMPVPGARYRDAHsGMSGPNAAMRRYLQAVTH 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 162 kaeengaPAVAMDIDAAG----LVTLA-LLGKPVGTK------------SI--EDLKEIISSTKLPVILKGVMTVEGAKK 222
Cdd:PRK11197 189 -------PQWAWDVGLNGrphdLGNISaYLGKPTGLEdyigwlgnnfdpSIswKDLEWIRDFWDGPMVIKGILDPEDARD 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 223 ALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADAVKGRMKIFVDGGFRTGLDIFKAIALGADAVLIGRPYAVAAYGGGA 302
Cdd:PRK11197 262 AVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIALGADTVLLGRAFVYALAAAGQ 341

                        330       340       350
                 ....*....|....*....|....*....|..
gi 501109392 303 EGVKVYTEKIGNELKETMIMAGCHNLADIKRD 334
Cdd:PRK11197 342 AGVANLLDLIEKEMRVAMTLTGAKSISEITRD 373
 
Name Accession Description Interval E-value
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 45-333 2.43e-94

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: 282.41  E-value: 2.43e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  45 FIRNWQKIQDVKINLDTIIEESPIDTSIELFGQKFTYPVFAAPIGAVGL-NYSPALDDFEYtkaiiggCKEAGvIGF--- 120
Cdd:cd02809   29 LRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLaHPDGELATARA-------AAAAG-IPFtls 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 121 TGDGVKDEfydlplQVVKENNGHG----IPTIKPWKKEEIIAKIKKAeenGAPAVAMDIDAAGLVTLallgkpvgtKSIE 196
Cdd:cd02809  101 TVSTTSLE------EVAAAAPGPRwfqlYVPRDREITEDLLRRAEAA---GYKALVLTVDTPVLGRR---------LTWD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 197 DLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADAVKGRMKIFVDGGFRTGLDI 276
Cdd:cd02809  163 DLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDV 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501109392 277 FKAIALGADAVLIGRPYAVAAYGGGAEGVKVYTEKIGNELKETMIMAGCHNLADIKR 333
Cdd:cd02809  243 LKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
FMN_dh pfam01070
FMN-dependent dehydrogenase;
47-336 5.31e-88

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 267.86  E-value: 5.31e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392   47 RNWQKIQDVKINLDTIIEESPIDTSIELFGQKFTYPVFAAPIGAVGLnYSPALDdfeytKAIIGGCKEAGVI----GFTG 122
Cdd:pfam01070  25 RNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGL-AHPDGE-----LALARAAAAAGIPfvlsTVSS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  123 DGVKDefydlplqVVKENNGHGIPTIKPWKKEEIIAK-IKKAEENGAPAVAMDIDAAGL--------------------V 181
Cdd:pfam01070  99 TSLEE--------VAAAAGGPLWFQLYVPRDRELTEDlLERAEAAGYKALVLTVDTPVLgrrerdlrngftlpprltprN 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  182 TLALLGKPVGTKSI-----------------------EDLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGG 238
Cdd:pfam01070 171 LLDLALHPRWALGVlrrggaggaaafvgsqfdpaltwDDLAWLRERWKGPLVVKGILSPEDAKRAVEAGVDGIVVSNHGG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  239 RVLDHTPATIEVLPAIADAVKGRMKIFVDGGFRTGLDIFKAIALGADAVLIGRPYAVAAYGGGAEGVKVYTEKIGNELKE 318
Cdd:pfam01070 251 RQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAHALEILRDELER 330

                         330
                  ....*....|....*...
gi 501109392  319 TMIMAGCHNLADIKRDRV 336
Cdd:pfam01070 331 TMALLGCKSIADLTPSLL 348
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 66-338 1.08e-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: 221.16  E-value: 1.08e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  66 SPIDTSIELFGQKFTYPVFAAPIGAVGL----------------------------------NYSPA--------LDDFE 103
Cdd:COG1304   57 SEIDLSTTLLGKRLAAPFLIAPMGGGGLahpdgelalaraaaaagipmglstqsttsleevaAAAPAplwfqlyvPKDRG 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 104 YTKAIIGGCKEAG--VIGFTgdgvkdefYDLPLQVVKEN---NGHGIP-TIKPWKKEEIIAKIKKAEENGAPAVAMDIDA 177
Cdd:COG1304  137 FTDDLLRRAEAAGadALVLT--------VDTPVLGRRERdlrEGFSQPpRLTPRNLLEAATHPRWALGLASLAAWLDTNF 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 178 AGLVTLallgkpvgtksiEDLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADA 257
Cdd:COG1304  209 DPSLTW------------DDIAWLRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAA 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 258 VKGRMKIFVDGGFRTGLDIFKAIALGADAVLIGRPYAVAAYGGGAEGVKVYTEKIGNELKETMIMAGCHNLADIKRDRVF 337
Cdd:COG1304  277 VGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356


                 .
gi 501109392 338 L 338
Cdd:COG1304  357 L 357
LMO_FMN cd03332
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ...
 69-336 2.99e-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: 177.09  E-value: 2.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  69 DTSIELFGQKFTYPVFAAPIGAVGLnyspALDDFEYTKAiiGGCKEAGViGFTGDGVKDEfydlPLQVVKENNGHGipti 148
Cdd:cd03332   74 DLSVELFGRTLAAPLLLAPIGVQEL----FHPDAELATA--RAAAELGV-PYILSTASSS----SIEDVAAAAGDA---- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 149 kP------WKKEEIIAK--IKKAEENGAPAVAM------------DIDAAGL---------------VTLALLGKPVG-- 191
Cdd:cd03332  139 -PrwfqlyWPKDDDLTEslLRRAEKAGYRVLVVtldtwslgwrprDLDLGYLpflrgigianyfsdpVFRKKLAEPVGed 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 192 ---------------------TKSIEDLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEV 250
Cdd:cd03332  218 peapppmeaavarfvsvfsgpSLTWEDLAFLREWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDA 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 251 LPAIADAVKGRMKIFVDGGFRTGLDIFKAIALGADAVLIGRPYAVAAYGGGAEGVKVYTEKIGNELKETMIMAGCHNLAD 330
Cdd:cd03332  298 LPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAE 377


                 ....*.
gi 501109392 331 IKRDRV 336
Cdd:cd03332  378 LTRDAL 383
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
 68-332 1.65e-48

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: 165.85  E-value: 1.65e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  68 IDTSIELFGQKFTYPVFAAPIGAVGLnyspALDDFEytKAIIGGCKEAGVIgftgdgvkdefydlplQVVKENNGHGIPT 147
Cdd:cd02922   52 VDTSTTILGHKVSLPFFISPAALAKL----AHPDGE--LNLARAAGKHGIL----------------QMISTNASCSLEE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 148 IKPWKKEEII---------------AKIKKAEENGAPAVAMDIDAAGL------------VTLALLGKPVGTK------- 193
Cdd:cd02922  110 IVDARPPDQPlffqlyvnkdrtkteELLKRAEKLGAKAIFLTVDAPVLgkrerderlkaeEAVSDGPAGKKTKakgggag 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 194 -----------SIEDLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEVLPAI---ADAVK 259
Cdd:cd02922  190 ramsgfidptlTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIrkhCPEVF 269

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501109392 260 GRMKIFVDGGFRTGLDIFKAIALGADAVLIGRP--YAVAAYggGAEGVKVYTEKIGNELKETMIMAGCHNLADIK 332
Cdd:cd02922  270 DKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPflYALSAY--GEEGVEKAIQILKDEIETTMRLLGVTSLDQLG 342
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 68-333 3.92e-45

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: 157.60  E-value: 3.92e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  68 IDTSIELFGQKFTYPVFAAPIGAVGLNYSPAlddfEYTKAiiGGCKEAGVIgFTGDGvkdeFYDLPLQVVKENNGHG--- 144
Cdd:cd04737   60 PDTSTELLGIKLKTPIIMAPIAAHGLAHATG----EVATA--RGMAEVGSL-FSIST----YSNTSLEEIAKASNGGpkw 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 145 --IPTIKPWK-KEEIIAKIKKAeenGAPAVAMDIDAAG-------------------LVTLALLGKPVGtKSI------- 195
Cdd:cd04737  129 fqLYMSKDDGfNRSLLDRAKAA---GAKAIILTADATVggnreadirnkfqfpfgmpNLNHFSEGTGKG-KGIseiyaaa 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 196 ------EDLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADAVKGRMKIFVDGG 269
Cdd:cd04737  205 kqklspADIEFIAKISGLPVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSG 284

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501109392 270 FRTGLDIFKAIALGADAVLIGRP--YAVAAygGGAEGVKVYTEKIGNELKETMIMAGCHNLADIKR 333
Cdd:cd04737  285 VRRGEHVFKALASGADAVAVGRPvlYGLAL--GGAQGVASVLEHLNKELKIVMQLAGTRTIEDVKR 348
lldD PRK11197
L-lactate dehydrogenase; Provisional
 47-334 8.02e-45

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 157.49  E-value: 8.02e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  47 RNWQKIQDVKINLDTIIEESPIDTSIELFGQKFTYPVFAAPIGAVGLN-------------------------------Y 95
Cdd:PRK11197  37 RNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGMYarrgevqaaraadakgipftlstvsvcpieeV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  96 SPA-----------LDDFEYTKAIIGGCKEAGV--IGFTgdgvkdefYDLPLQVVKENNGH-GIPTIKPWKKEEIIAKIK 161
Cdd:PRK11197 117 APAikrpmwfqlyvLRDRGFMRNALERAKAAGCstLVFT--------VDMPVPGARYRDAHsGMSGPNAAMRRYLQAVTH 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 162 kaeengaPAVAMDIDAAG----LVTLA-LLGKPVGTK------------SI--EDLKEIISSTKLPVILKGVMTVEGAKK 222
Cdd:PRK11197 189 -------PQWAWDVGLNGrphdLGNISaYLGKPTGLEdyigwlgnnfdpSIswKDLEWIRDFWDGPMVIKGILDPEDARD 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 223 ALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADAVKGRMKIFVDGGFRTGLDIFKAIALGADAVLIGRPYAVAAYGGGA 302
Cdd:PRK11197 262 AVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIALGADTVLLGRAFVYALAAAGQ 341

                        330       340       350
                 ....*....|....*....|....*....|..
gi 501109392 303 EGVKVYTEKIGNELKETMIMAGCHNLADIKRD 334
Cdd:PRK11197 342 AGVANLLDLIEKEMRVAMTLTGAKSISEITRD 373
PLN02535 PLN02535
glycolate oxidase
 193-336 3.68e-42

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 149.99  E-value: 3.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 193 KSIEDLKEIissTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADAVKGRMKIFVDGGFRT 272
Cdd:PLN02535 213 KDIEWLRSI---TNLPILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRR 289

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501109392 273 GLDIFKAIALGADAVLIGRP--YAVAAygGGAEGVKVYTEKIGNELKETMIMAGCHNLADIKRDRV 336
Cdd:PLN02535 290 GTDVFKALALGAQAVLVGRPviYGLAA--KGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHV 353
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
 192-336 1.38e-37

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


Pssm-ID: 166134 [Multi-domain]  Cd Length: 367  Bit Score: 137.94  E-value: 1.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 192 TKSIEDLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADAVKGRMKIFVDGGFR 271
Cdd:PLN02493 210 TLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVR 289

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501109392 272 TGLDIFKAIALGADAVLIGRPYAVAAYGGGAEGVKVYTEKIGNELKETMIMAGCHNLADIKRDRV 336
Cdd:PLN02493 290 RGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 354
PLN02979 PLN02979
glycolate oxidase
 192-336 2.97e-37

glycolate oxidase


Pssm-ID: 166620  Cd Length: 366  Bit Score: 137.16  E-value: 2.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 192 TKSIEDLKEIISSTKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADAVKGRMKIFVDGGFR 271
Cdd:PLN02979 209 TLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVR 288

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501109392 272 TGLDIFKAIALGADAVLIGRPYAVAAYGGGAEGVKVYTEKIGNELKETMIMAGCHNLADIKRDRV 336
Cdd:PLN02979 289 RGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 353
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
 209-333 4.56e-27

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: 109.15  E-value: 4.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 209 VILKGVMTVEGAKKALKAGAYGIVVSNHGGRVLDHTPATIEVLPAIADAVKgrMKIFVDGGFRTGLDIFKAIALGADAVL 288
Cdd:cd04736  239 LLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATY--KPVLIDSGIRRGSDIVKALALGANAVL 316

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501109392 289 IGRP--YAVAAygGGAEGVKVYTEKIGNELKETMIMAGCHNLADIKR 333
Cdd:cd04736  317 LGRAtlYGLAA--RGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 68-333 1.26e-19

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: 87.94  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  68 IDTSIELFGQKFTYPVFaapIGAV--GlnySPALDDFEYTKAIIggCKEAGV--------IGFTGDGVKDEFydlplQVV 137
Cdd:cd02811   40 IDLSTEFLGKRLSAPLL---ISAMtgG---SEKAKEINRNLAEA--AEELGIamgvgsqrAALEDPELAESF-----TVV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 138 KENNGHGIptikpwkkeeIIAKIKKAEENGAP------AVAMdIDAAGL-VTLALL-------GKPVGTKSIEDLKEIIS 203
Cdd:cd02811  107 REAPPNGP----------LIANLGAVQLNGYGveearrAVEM-IEADALaIHLNPLqeavqpeGDRDFRGWLERIEELVK 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 204 STKLPVILKGV---MTVEGAKKALKAGAYGIVVSNHGG---------RVLDH--------------TPATI-EVLPAIAD 256
Cdd:cd02811  176 ALSVPVIVKEVgfgISRETAKRLADAGVKAIDVAGAGGtswarvenyRAKDSdqrlaeyfadwgipTAASLlEVRSALPD 255

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501109392 257 AvkgrmKIFVDGGFRTGLDIFKAIALGADAVLIGRPYAVAAYgGGAEGVKVYTEKIGNELKETMIMAGCHNLADIKR 333
Cdd:cd02811  256 L-----PLIASGGIRNGLDIAKALALGADLVGMAGPFLKAAL-EGEEAVIETIEQIIEELRTAMFLTGAKNLAELKQ 326
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
 195-334 7.44e-13

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: 68.72  E-value: 7.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 195 IEDLKEIisSTKLPVILK-----GVMTVEGAKKalKAGAYGIVVSNHGG-------RVLDHtpATIEVLPAIADAV---- 258
Cdd:cd02808  205 IEDLREA--TGGKPIGVKlvaghGEGDIAAGVA--AAGADFITIDGAEGgtgaaplTFIDH--VGLPTELGLARAHqalv 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 259 ----KGRMKIFVDGGFRTGLDIFKAIALGADAVLIGR-------------------PYAVAAY----------GGGAEGV 305
Cdd:cd02808  279 knglRDRVSLIASGGLRTGADVAKALALGADAVGIGTaalialgciqarkchtntcPVGVATQdpelrrrldvEGKAERV 358

                        170       180       190
                 ....*....|....*....|....*....|.
gi 501109392 306 KVYTEKIGNELKEtmIMAGC--HNLADIKRD 334
Cdd:cd02808  359 ANYLKSLAEELRE--LAAALgkRSLELLGRS 387
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
 194-296 4.18e-12

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: 66.20  E-value: 4.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  194 SIEDLKEIISSTK-----LPVILK-----GVMTVegAKKALKAGAYGIVVSNHGG-------RVLDHTPATIEVlpAIAD 256
Cdd:pfam01645 185 SIEDLAQLIYDLKeinpkAPISVKlvsghGVGTI--AAGVAKAGADIILIDGYDGgtgaspkTSIKHAGLPWEL--ALAE 260

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 501109392  257 AVKG--------RMKIFVDGGFRTGLDIFKAIALGADAVLIGRPYAVA 296
Cdd:pfam01645 261 AHQTlkenglrdRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIA 308
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 195-318 6.97e-09

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: 56.37  E-value: 6.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 195 IEDLKEIISstKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGGRVldHTpaTIEV-------LPAIADAVKGRMKIFV- 266
Cdd:cd00381  126 IKFIKKKYP--NVDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSI--CT--TRIVtgvgvpqATAVADVAAAARDYGVp 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 501109392 267 ---DGGFRTGLDIFKAIALGADAVLIGRPYAvaaygGGAEGVKVYTEKIGNELKE 318
Cdd:cd00381  200 viaDGGIRTSGDIVKALAAGADAVMLGSLLA-----GTDESPGEYIEINGKRYKE 249
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 216-290 2.93e-08

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 54.35  E-value: 2.93e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501109392 216 TVEGAKKALKAGAYGIVVSNH--GGRVLDHTPATIEVLPAIADAVKGrmKIFVDGGFRTGLDIFKAIALGADAVLIG 290
Cdd:COG2070  113 SVREARKAEKAGADAVVAEGAeaGGHRGADEVSTFALVPEVRDAVDI--PVIAAGGIADGRGIAAALALGADGVQMG 187
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 214-290 3.68e-08

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: 53.26  E-value: 3.68e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501109392 214 VMTVEGAKKALKAGAYGIVVSNH--GGRVLDHTPATIEVLPAIADAVKGrmKIFVDGGFRTGLDIFKAIALGADAVLIG 290
Cdd:cd04730  109 VTSVEEARKAEAAGADALVAQGAeaGGHRGTFDIGTFALVPEVRDAVDI--PVIAAGGIADGRGIAAALALGADGVQMG 185
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 195-291 1.11e-07

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: 51.43  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 195 IEDLKEIISStkLPVILKGVMTVEGAKKALK-AGAYGIVVSNHGGRVLDHTPATIEVLPAIADAVKGRMKIFVDGGFRTG 273
Cdd:cd04722  105 IRELREAVPD--VKVVVKLSPTGELAAAAAEeAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDP 182

                         90
                 ....*....|....*...
gi 501109392 274 LDIFKAIALGADAVLIGR 291
Cdd:cd04722  183 EDAAEALALGADGVIVGS 200
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ...
 195-291 2.67e-07

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: 52.17  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 195 IEDLKEIisSTKLPVILK-----GVMTVEGAKKALKAGAYG--IVVSNH-GG-----RVL-DH--TPATiEVLPAIADA- 257
Cdd:COG0069  356 IFDLREL--NPGAPVGVKlvsgaGVGTIAACKGVAKTGAYAdfITIDGGeGGtgaapLESiKHagLPWE-LGLAEVHQTl 432

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501109392 258 ----VKGRMKIFVDGGFRTGLDIFKAIALGADAVLIGR 291
Cdd:COG0069  433 vgngLRDRIRLIADGKLKTGRDVAIAAALGADEFGFAR 470
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 153-291 7.07e-05

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 44.19  E-value: 7.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 153 KEEIIAKIKKAEENGAPAVAMDIdAAGLVTLAllgkpvgtksIEDLKEIISST-KLPVILKGVMTVEGAKKALKAGAYGI 231
Cdd:PTZ00314 239 RPEDIERAAALIEAGVDVLVVDS-SQGNSIYQ----------IDMIKKLKSNYpHVDIIAGNVVTADQAKNLIDAGADGL 307

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501109392 232 VVSNHGGRVLdhtpATIEVLP---AIADAV--------KGRMKIFVDGGFRTGLDIFKAIALGADAVLIGR 291
Cdd:PTZ00314 308 RIGMGSGSIC----ITQEVCAvgrPQASAVyhvaryarERGVPCIADGGIKNSGDICKALALGADCVMLGS 374
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
 156-294 9.97e-05

IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440282 [Multi-domain]  Cd Length: 326  Bit Score: 43.66  E-value: 9.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 156 IIAKIKKAEENGAPAVAMDIDAAGLVTLALLGKPVGTKSIEDLKEiiSSTKLPVILKGVMTVEGAKKALKAGAYGIVVSN 235
Cdd:COG0516   88 VLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGGDAMKKIKL--TFDDVLLIPGNSATVEPARALVDAGADLTKVGI 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501109392 236 HGGRVlDHTPATIEV----LPAIADAVKG-RMKIFV--DGGFRTGLDIFKAIALGADAVLIGRPYA 294
Cdd:COG0516  166 GPGSI-CTTRVVIGLgipqLSAAMDTVTEaRMAIAIaaDGGIGYIHDNAKALAAGADAVMLGSLFA 230
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 153-290 7.54e-04

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: 40.80  E-value: 7.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 153 KEEIIAKIKKAEENGAPAVAMDI---DAAGLVTLALLGKPVgtksIEDLKEIISSTKLPVILK-GVMT-----VEGAKKA 223
Cdd:cd02810  110 KEDYVELARKIERAGAKALELNLscpNVGGGRQLGQDPEAV----ANLLKAVKAAVDIPLLVKlSPYFdlediVELAKAA 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 224 LKAGAYGIVVSNH-GGRVLDHT-------------------PATIEVLPAIADAVKGRMKIFVDGGFRTGLDIFKAIALG 283
Cdd:cd02810  186 ERAGADGLTAINTiSGRVVDLKtvgpgpkrgtgglsgapirPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAG 265


                 ....*..
gi 501109392 284 ADAVLIG 290
Cdd:cd02810  266 ASAVQVA 272
PRK06843 PRK06843
inosine 5-monophosphate dehydrogenase; Validated
 170-294 9.61e-04

inosine 5-monophosphate dehydrogenase; Validated


Pssm-ID: 180725 [Multi-domain]  Cd Length: 404  Bit Score: 40.79  E-value: 9.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 170 AVAMDIDA--------AGLVTLALLGKPVG--TKSIEDLKEIisSTKLP---VILKGVMTVEGAKKALKAGAYGIVVSNH 236
Cdd:PRK06843 147 AVSIDIDTierveelvKAHVDILVIDSAHGhsTRIIELVKKI--KTKYPnldLIAGNIVTKEAALDLISVGADCLKVGIG 224

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501109392 237 GGRV-LDHTPATIEV--LPAIADAVK----GRMKIFVDGGFRTGLDIFKAIALGADAVLIGRPYA 294
Cdd:PRK06843 225 PGSIcTTRIVAGVGVpqITAICDVYEvcknTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFA 289
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 259-332 1.82e-03

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 39.55  E-value: 1.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501109392 259 KGRMKIFVDGGFRTGLDIFKAIALGADAVLIGRPYAvaaygggAEGVKVYtEKIGNELKETMIMAGCHNLADIK 332
Cdd:PRK02506 239 NPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALH-------KEGPAVF-ERLTKELKAIMAEKGYQSLEDFR 304
thiG CHL00162
thiamin biosynthesis protein G; Validated
 166-233 3.07e-03

thiamin biosynthesis protein G; Validated


Pssm-ID: 214380  Cd Length: 267  Bit Score: 38.92  E-value: 3.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501109392 166 NGAPAVAMDIDAAGLVTLALLGKPVGT----KSIEDLKEIISSTKLPVILK-GVMTVEGAKKALKAGAYGIVV 233
Cdd:CHL00162 145 NADPMLAKHLEDIGCATVMPLGSPIGSgqglQNLLNLQIIIENAKIPVIIDaGIGTPSEASQAMELGASGVLL 217
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 195-291 3.77e-03

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 38.91  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392  195 IEDLKEIISS-TKLPVILKGVMTVEGAKKALKAGAYGIVVSNHGG-----RVLdhtpATIEV--LPAIADAVKGRMK--- 263
Cdd:pfam00478 249 IDTVKWIKKKyPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPGsicttRVV----AGVGVpqLTAIYDVAEAAKKygv 324

                          90       100
                  ....*....|....*....|....*....
gi 501109392  264 -IFVDGGFRTGLDIFKAIALGADAVLIGR 291
Cdd:pfam00478 325 pVIADGGIKYSGDIVKALAAGADAVMLGS 353
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 184-299 4.80e-03

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: 37.86  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 184 ALLGKPVGTKSIedLKEIISSTKLPVILK-------GVMTVEGAKKALKAGAYGIVVsnHGGRVLD--HTPATIEVLPAI 254
Cdd:cd02801  103 ALLKDPELVAEI--VRAVREAVPIPVTVKirlgwddEEETLELAKALEDAGASALTV--HGRTREQrySGPADWDYIAEI 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 501109392 255 ADAVKgrMKIFVDGGFRTGLDIFKAIAL-GADAVLIGRpyavAAYG 299
Cdd:cd02801  179 KEAVS--IPVIANGDIFSLEDALRCLEQtGVDGVMIGR----GALG 218
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
154-233 5.07e-03

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 37.82  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 154 EEIIAKIKkaEENGAPAVAmDID---------AAG--LVTLALLGKPVGTKSIED-----LKEIISSTKLPVILKG-VMT 216
Cdd:PRK01130 108 AELVKRIK--EYPGQLLMA-DCStleeglaaqKLGfdFIGTTLSGYTEETKKPEEpdfalLKELLKAVGCPVIAEGrINT 184

                         90
                 ....*....|....*..
gi 501109392 217 VEGAKKALKAGAYGIVV 233
Cdd:PRK01130 185 PEQAKKALELGAHAVVV 201
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 239-295 8.22e-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: 37.58  E-value: 8.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501109392 239 RVLDHTPATIEVlpaIADAVKGRMKIFVDGGFRTGLDIFKAIALGADAVLIGRPYAV 295
Cdd:cd04735  265 RGRDDNQTIMEL---VKERIAGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLV 318
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 154-233 9.23e-03

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 36.78  E-value: 9.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501109392 154 EEIIAKIKkaEENGAPAVAmDID---------AAG--LVTLALLGKPVGTKSIED-----LKEIISSTKLPVILKG-VMT 216
Cdd:cd04729  112 AELIKRIH--EEYNCLLMA-DIStleealnaaKLGfdIIGTTLSGYTEETAKTEDpdfelLKELRKALGIPVIAEGrINS 188

                         90
                 ....*....|....*..
gi 501109392 217 VEGAKKALKAGAYGIVV 233
Cdd:cd04729  189 PEQAAKALELGADAVVV 205
 
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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