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Conserved domains on  [gi|568959277|ref|XP_006510286|]
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FAD-dependent oxidoreductase domain-containing protein 1 isoform X1 [Mus musculus]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11429741)

FAD/NAD(P)-binding oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.30.9.10
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0050660

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
62-405 2.88e-31

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


:

Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 122.71  E-value: 2.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277  62 EQADVVIIGGGILGLSVAFWLkkleSRRGAiRVLVVEQDHTYSRASSTgpSVGGIWQQFS---VPENVQLSLFSINFLRn 138
Cdd:COG0665    1 ATADVVVIGGGIAGLSTAYHL----ARRGL-DVTVLERGRPGSGASGR--NAGQLRPGLAalaDRALVRLAREALDLWR- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 139 ineylAVVDAPPVELQFNPSGCLLLA-SEKDAATLENNVKMQRFHHfiYPNEdpnwgtcSLEKDQQCpcenGQEPGVSTS 217
Cdd:COG0665   73 -----ELAAELGIDCDFRRTGVLYLArTEAELAALRAEAEALRALG--LPVE-------LLDAAELR----EREPGLGSP 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 218 R-----------MCCSDQCCRSL----------VWENCRAgwcwegTSWHPPGHQAT-----------------CGA--- 256
Cdd:COG0665  135 DyagglydpddgHVDPAKLVRALaraaraagvrIREGTPV------TGLEREGGRVTgvrtergtvradavvlaAGAwsa 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 257 ----------------------KEKGPGLETPLVADiSGVYFRREGLGSNYLGGcspteEEEPDPTNLNVDHDFFQnKVW 314
Cdd:COG0665  209 rllpmlglrlplrpvrgyvlvtEPLPDLPLRPVLDD-TGVYLRPTADGRLLVGG-----TAEPAGFDRAPTPERLE-ALL 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 315 PHLVQRVPSFKTLEhllhlqVQSAWAGYYDYnTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHfK 394
Cdd:COG0665  282 RRLRRLFPALADAE------IVRAWAGLRPM-TPDGLPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGE-P 353

                        410
                 ....*....|.
gi 568959277 395 TIDMSPFLFTR 405
Cdd:COG0665  354 PLDLAPFSPDR 364
 
Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
62-405 2.88e-31

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 122.71  E-value: 2.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277  62 EQADVVIIGGGILGLSVAFWLkkleSRRGAiRVLVVEQDHTYSRASSTgpSVGGIWQQFS---VPENVQLSLFSINFLRn 138
Cdd:COG0665    1 ATADVVVIGGGIAGLSTAYHL----ARRGL-DVTVLERGRPGSGASGR--NAGQLRPGLAalaDRALVRLAREALDLWR- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 139 ineylAVVDAPPVELQFNPSGCLLLA-SEKDAATLENNVKMQRFHHfiYPNEdpnwgtcSLEKDQQCpcenGQEPGVSTS 217
Cdd:COG0665   73 -----ELAAELGIDCDFRRTGVLYLArTEAELAALRAEAEALRALG--LPVE-------LLDAAELR----EREPGLGSP 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 218 R-----------MCCSDQCCRSL----------VWENCRAgwcwegTSWHPPGHQAT-----------------CGA--- 256
Cdd:COG0665  135 DyagglydpddgHVDPAKLVRALaraaraagvrIREGTPV------TGLEREGGRVTgvrtergtvradavvlaAGAwsa 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 257 ----------------------KEKGPGLETPLVADiSGVYFRREGLGSNYLGGcspteEEEPDPTNLNVDHDFFQnKVW 314
Cdd:COG0665  209 rllpmlglrlplrpvrgyvlvtEPLPDLPLRPVLDD-TGVYLRPTADGRLLVGG-----TAEPAGFDRAPTPERLE-ALL 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 315 PHLVQRVPSFKTLEhllhlqVQSAWAGYYDYnTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHfK 394
Cdd:COG0665  282 RRLRRLFPALADAE------IVRAWAGLRPM-TPDGLPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGE-P 353

                        410
                 ....*....|.
gi 568959277 395 TIDMSPFLFTR 405
Cdd:COG0665  354 PLDLAPFSPDR 364
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 65-387 1.26e-22

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 97.85  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277   65 DVVIIGGGILGLSVAFWLkkleSRRGaIRVLVVEQDHTYSRASSTGPSvGGIWQQFSVPEN---VQLSLFSINFLRNINE 141
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYEL----ARRG-LSVTLLERGDDPGSGASGRNA-GLIHPGLRYLEPselARLALEALDLWEELEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277  142 YLAvvdappVELQFNPSGCLLLASEKDAATLENNVKMQRFHHF------------IYPNED--------PNWGTC----- 196
Cdd:pfam01266  75 ELG------IDCGFRRCGVLVLARDEEEEALEKLLAALRRLGVpaelldaeelreLEPLLPglrgglfyPDGGHVdparl 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277  197 --SLEKD---------QQCPC----ENGQEPGVSTSRmccsdqCCRSLVweNCRAGWC--WEGTSWHPPG------HQAT 253
Cdd:pfam01266 149 lrALARAaealgvriiEGTEVtgieEEGGVWGVVTTG------EADAVV--NAAGAWAdlLALPGLRLPVrpvrgqVLVL 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277  254 CGAKEKGPGLETP-LVADISGVYFRREGLGSNYLGGcsptEEEEPDPTNLNVDHDFFQnKVWPHLVQRVPSFKTLEHllh 332
Cdd:pfam01266 221 EPLPEALLILPVPiTVDPGRGVYLRPRADGRLLLGG----TDEEDGFDDPTPDPEEIE-ELLEAARRLFPALADIER--- 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568959277  333 lqvqsAWAGYYDynTFDQNGVVGPhPLVVNMYFATGFSGRGLQHAPGIGRAVAEI 387
Cdd:pfam01266 293 -----AWAGLRP--LPDGLPIIGR-PGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
solA PRK11259
N-methyl-L-tryptophan oxidase;
343-406 1.49e-06

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 49.83  E-value: 1.49e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568959277 343 YDyNTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHFKtIDMSPFLFTRF 406
Cdd:PRK11259 313 YT-NTPDEHFIIDTLPGHPNVLVASGCSGHGFKFASVLGEILADLAQDGTSD-FDLSPFSLSRF 374
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
 346-406 7.91e-05

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 44.44  E-value: 7.91e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568959277  346 NTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHfKTIDMSPFLFTRF 406
Cdd:TIGR01377 315 NTPDEHFVIDLHPKYDNVVIGAGFSGHGFKLAPVVGKILAELAMKLK-PSYDLAIFSLNRF 374
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 64-98 9.02e-03

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 38.06  E-value: 9.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 568959277  64 ADVVIIGGGILGLSVAFWLKklesRRGAIRVLVVE 98
Cdd:cd08262  163 EVALVIGCGPIGLAVIAALK----ARGVGPIVASD 193
 
Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
62-405 2.88e-31

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 122.71  E-value: 2.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277  62 EQADVVIIGGGILGLSVAFWLkkleSRRGAiRVLVVEQDHTYSRASSTgpSVGGIWQQFS---VPENVQLSLFSINFLRn 138
Cdd:COG0665    1 ATADVVVIGGGIAGLSTAYHL----ARRGL-DVTVLERGRPGSGASGR--NAGQLRPGLAalaDRALVRLAREALDLWR- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 139 ineylAVVDAPPVELQFNPSGCLLLA-SEKDAATLENNVKMQRFHHfiYPNEdpnwgtcSLEKDQQCpcenGQEPGVSTS 217
Cdd:COG0665   73 -----ELAAELGIDCDFRRTGVLYLArTEAELAALRAEAEALRALG--LPVE-------LLDAAELR----EREPGLGSP 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 218 R-----------MCCSDQCCRSL----------VWENCRAgwcwegTSWHPPGHQAT-----------------CGA--- 256
Cdd:COG0665  135 DyagglydpddgHVDPAKLVRALaraaraagvrIREGTPV------TGLEREGGRVTgvrtergtvradavvlaAGAwsa 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 257 ----------------------KEKGPGLETPLVADiSGVYFRREGLGSNYLGGcspteEEEPDPTNLNVDHDFFQnKVW 314
Cdd:COG0665  209 rllpmlglrlplrpvrgyvlvtEPLPDLPLRPVLDD-TGVYLRPTADGRLLVGG-----TAEPAGFDRAPTPERLE-ALL 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277 315 PHLVQRVPSFKTLEhllhlqVQSAWAGYYDYnTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHfK 394
Cdd:COG0665  282 RRLRRLFPALADAE------IVRAWAGLRPM-TPDGLPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGE-P 353

                        410
                 ....*....|.
gi 568959277 395 TIDMSPFLFTR 405
Cdd:COG0665  354 PLDLAPFSPDR 364
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 65-387 1.26e-22

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 97.85  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277   65 DVVIIGGGILGLSVAFWLkkleSRRGaIRVLVVEQDHTYSRASSTGPSvGGIWQQFSVPEN---VQLSLFSINFLRNINE 141
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYEL----ARRG-LSVTLLERGDDPGSGASGRNA-GLIHPGLRYLEPselARLALEALDLWEELEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277  142 YLAvvdappVELQFNPSGCLLLASEKDAATLENNVKMQRFHHF------------IYPNED--------PNWGTC----- 196
Cdd:pfam01266  75 ELG------IDCGFRRCGVLVLARDEEEEALEKLLAALRRLGVpaelldaeelreLEPLLPglrgglfyPDGGHVdparl 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277  197 --SLEKD---------QQCPC----ENGQEPGVSTSRmccsdqCCRSLVweNCRAGWC--WEGTSWHPPG------HQAT 253
Cdd:pfam01266 149 lrALARAaealgvriiEGTEVtgieEEGGVWGVVTTG------EADAVV--NAAGAWAdlLALPGLRLPVrpvrgqVLVL 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277  254 CGAKEKGPGLETP-LVADISGVYFRREGLGSNYLGGcsptEEEEPDPTNLNVDHDFFQnKVWPHLVQRVPSFKTLEHllh 332
Cdd:pfam01266 221 EPLPEALLILPVPiTVDPGRGVYLRPRADGRLLLGG----TDEEDGFDDPTPDPEEIE-ELLEAARRLFPALADIER--- 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568959277  333 lqvqsAWAGYYDynTFDQNGVVGPhPLVVNMYFATGFSGRGLQHAPGIGRAVAEI 387
Cdd:pfam01266 293 -----AWAGLRP--LPDGLPIIGR-PGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
solA PRK11259
N-methyl-L-tryptophan oxidase;
343-406 1.49e-06

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 49.83  E-value: 1.49e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568959277 343 YDyNTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHFKtIDMSPFLFTRF 406
Cdd:PRK11259 313 YT-NTPDEHFIIDTLPGHPNVLVASGCSGHGFKFASVLGEILADLAQDGTSD-FDLSPFSLSRF 374
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
62-99 1.62e-06

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 49.76  E-value: 1.62e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568959277  62 EQADVVIIGGGILGLSVAFWLKKLESRrgaiRVLVVEQ 99
Cdd:COG0579    3 EMYDVVIIGAGIVGLALARELSRYEDL----KVLVLEK 36
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 63-116 1.65e-05

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 46.75  E-value: 1.65e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568959277  63 QADVVIIGGGILGLSVAFWLKKLesrrgAIRVLVVEQDhtysrasstgPSVGGI 116
Cdd:COG1232    1 MKRVAVIGGGIAGLTAAYRLAKA-----GHEVTVLEAS----------DRVGGL 39
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 60-120 3.35e-05

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 45.62  E-value: 3.35e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568959277  60 PPEQADVVIIGGGILGLSVAFWLKklesRRGaIRVLVVEQdhtysrasstGPSVGGIWQQF 120
Cdd:COG2072    3 ATEHVDVVVIGAGQAGLAAAYHLR----RAG-IDFVVLEK----------ADDVGGTWRDN 48
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 61-120 4.15e-05

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 45.31  E-value: 4.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568959277  61 PEQADVVIIGGGILGLSVAFWLKklesRRGaIRVLVVEQD---HTYSRASSTGP-SVG-----GIWQQF 120
Cdd:COG0654    1 MMRTDVLIVGGGPAGLALALALA----RAG-IRVTVVERApppRPDGRGIALSPrSLEllrrlGLWDRL 64
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
 346-406 7.91e-05

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 44.44  E-value: 7.91e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568959277  346 NTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHfKTIDMSPFLFTRF 406
Cdd:TIGR01377 315 NTPDEHFVIDLHPKYDNVVIGAGFSGHGFKLAPVVGKILAELAMKLK-PSYDLAIFSLNRF 374
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
65-98 2.27e-04

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 43.27  E-value: 2.27e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 568959277  65 DVVIIGGGILGLSVAFWLkkLESRRGAiRVLVVE 98
Cdd:PRK11728   4 DFVIIGGGIVGLSTAMQL--QERYPGA-RIAVLE 34
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 65-117 3.65e-04

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 42.66  E-value: 3.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568959277   65 DVVIIGGGILGLSVAfwlkkLESRRGAIRVLVVEQdhTYSRASSTGPSVGGIW 117
Cdd:pfam00890   1 DVLVIGGGLAGLAAA-----LAAAEAGLKVAVVEK--GQPFGGATAWSSGGID 46
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 62-116 5.64e-04

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 42.27  E-value: 5.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568959277  62 EQADVVIIGGGILGLSVAfwlkkLESRRGAIRVLVVEQDHTysRASSTGPSVGGI 116
Cdd:PRK07804  15 DAADVVVVGSGVAGLTAA-----LAARRAGRRVLVVTKAAL--DDGSTRWAQGGI 62
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 62-117 5.99e-04

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 41.74  E-value: 5.99e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568959277  62 EQADVVIIGGGILGLSVAfwlkkLESRRGAIRVLVVEQDHTY---SRASStgpsvGGIW 117
Cdd:COG1053    2 HEYDVVVVGSGGAGLRAA-----LEAAEAGLKVLVLEKVPPRgghTAAAQ-----GGIN 50
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 66-101 6.88e-04

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 41.76  E-value: 6.88e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 568959277  66 VVIIGGGILGLSVAFWLKKLESrrgAIRVLVVEQDH 101
Cdd:PRK11883   3 VAIIGGGITGLSAAYRLHKKGP---DADITLLEASD 35
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 64-100 2.06e-03

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 40.20  E-value: 2.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568959277   64 ADVVIIGGGILGLSVAFWLKKlESRRGAIRVLVVEQD 100
Cdd:TIGR00562   3 KHVVIIGGGISGLCAAYYLEK-EIPELPVELTLVEAS 38
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
56-106 4.83e-03

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 39.12  E-value: 4.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568959277  56 TSHLPPEQADVVIIGGGILGLSVAFWLkkleSRRGaIRVLVVEQDHT---YSRA 106
Cdd:PRK06183   3 AQHPDAHDTDVVIVGAGPVGLTLANLL----GQYG-VRVLVLERWPTlydLPRA 51
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 17-173 5.50e-03

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 39.06  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277  17 RGLRtrKGGFTLdwdAKVSDFKKKVDsILPGKKYEVLYDTSHLP-------PEQADVVIIGGGILGLSVAFWLkkleSRR 89
Cdd:PRK01747 213 RGLQ--EAGFTV---RKVKGFGRKRE-MLVGELEQTLPAPLAAPwfarpgsPKARDAAIIGGGIAGAALALAL----ARR 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568959277  90 GAiRVLVVEQDHTYSRASStGPSVGGIWQQFSVPENVqLSLFSIN-FLRNINEYLAVVDApPVELQFNPSGCLLLA-SEK 167
Cdd:PRK01747 283 GW-QVTLYEADEAPAQGAS-GNRQGALYPLLSKDDNA-LSRFFRAaFLFARRFYDALPAA-GVAFDHDWCGVLQLAwDEK 358


                 ....*.
gi 568959277 168 DAATLE 173
Cdd:PRK01747 359 SAEKIA 364
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 65-99 8.35e-03

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 38.29  E-value: 8.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 568959277  65 DVVIIGGGILGLSVAFWLkkleSRRGAiRVLVVEQ 99
Cdd:COG1233    5 DVVVIGAGIGGLAAAALL----ARAGY-RVTVLEK 34
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 64-98 9.02e-03

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 38.06  E-value: 9.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 568959277  64 ADVVIIGGGILGLSVAFWLKklesRRGAIRVLVVE 98
Cdd:cd08262  163 EVALVIGCGPIGLAVIAALK----ARGVGPIVASD 193
 
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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