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Conserved domains on  [gi|1039792903|ref|XP_017168798|]
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FAD-dependent oxidoreductase domain-containing protein 1 isoform X2 [Mus musculus]

Protein Classification

FAD-binding oxidoreductase( domain architecture ID 11429741)

FAD-binding oxidoreductase catalyzes the oxidation or reduction of a specific substrate using flavin adenine dinucleotide (FAD) as a cofactor

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0016491
SCOP:  3000055

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];
62-399 1.06e-33

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


:

Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 129.25  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903  62 EQADVVIIGGGILGLSVAFWLkkleSRRGAiRVLVVEQDHTYSRASSTgpSVGGIWQQFS---VPENVQLSLFSINFLRn 138
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHL----ARRGL-DVTVLERGRPGSGASGR--NAGQLRPGLAalaDRALVRLAREALDLWR- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 139 ineylAVVDAPPVELQFNPSGCLLLA-SEKDAATLENNVKMQRFHHfiYPNEdpnwgtcSLEKDQQCpcenGQEPGVSTS 217
Cdd:COG0665    73 -----ELAAELGIDCDFRRTGVLYLArTEAELAALRAEAEALRALG--LPVE-------LLDAAELR----EREPGLGSP 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 218 R-----------MCCSDQCCRSL----------VWENCRAgwcwegTSWHPPGHQAT-----------------CGA--- 256
Cdd:COG0665   135 DyagglydpddgHVDPAKLVRALaraaraagvrIREGTPV------TGLEREGGRVTgvrtergtvradavvlaAGAwsa 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 257 ----------------------KEKGPGLETPLVADiSGVYFRREGLGSNYLGGcspteEEEPDPTNLNVDHDFFQnKVW 314
Cdd:COG0665   209 rllpmlglrlplrpvrgyvlvtEPLPDLPLRPVLDD-TGVYLRPTADGRLLVGG-----TAEPAGFDRAPTPERLE-ALL 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 315 PHLVQRVPSFKTLEVQSAWAGYYDYnTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHfKTIDMSP 394
Cdd:COG0665   282 RRLRRLFPALADAEIVRAWAGLRPM-TPDGLPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGE-PPLDLAP 359


                  ....*
gi 1039792903 395 FLFTR 399
Cdd:COG0665   360 FSPDR 364
 
Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
62-399 1.06e-33

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 129.25  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903  62 EQADVVIIGGGILGLSVAFWLkkleSRRGAiRVLVVEQDHTYSRASSTgpSVGGIWQQFS---VPENVQLSLFSINFLRn 138
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHL----ARRGL-DVTVLERGRPGSGASGR--NAGQLRPGLAalaDRALVRLAREALDLWR- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 139 ineylAVVDAPPVELQFNPSGCLLLA-SEKDAATLENNVKMQRFHHfiYPNEdpnwgtcSLEKDQQCpcenGQEPGVSTS 217
Cdd:COG0665    73 -----ELAAELGIDCDFRRTGVLYLArTEAELAALRAEAEALRALG--LPVE-------LLDAAELR----EREPGLGSP 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 218 R-----------MCCSDQCCRSL----------VWENCRAgwcwegTSWHPPGHQAT-----------------CGA--- 256
Cdd:COG0665   135 DyagglydpddgHVDPAKLVRALaraaraagvrIREGTPV------TGLEREGGRVTgvrtergtvradavvlaAGAwsa 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 257 ----------------------KEKGPGLETPLVADiSGVYFRREGLGSNYLGGcspteEEEPDPTNLNVDHDFFQnKVW 314
Cdd:COG0665   209 rllpmlglrlplrpvrgyvlvtEPLPDLPLRPVLDD-TGVYLRPTADGRLLVGG-----TAEPAGFDRAPTPERLE-ALL 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 315 PHLVQRVPSFKTLEVQSAWAGYYDYnTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHfKTIDMSP 394
Cdd:COG0665   282 RRLRRLFPALADAEIVRAWAGLRPM-TPDGLPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGE-PPLDLAP 359


                  ....*
gi 1039792903 395 FLFTR 399
Cdd:COG0665   360 FSPDR 364
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 65-381 1.59e-23

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: 100.55  E-value: 1.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903  65 DVVIIGGGILGLSVAFWLkkleSRRGaIRVLVVEQDHTYSRASSTGPSvGGIWQQFSVPEN---VQLSLFSINFLRNINE 141
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYEL----ARRG-LSVTLLERGDDPGSGASGRNA-GLIHPGLRYLEPselARLALEALDLWEELEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 142 YLAVvdappvELQFNPSGCLLLASEKDAATLENNVKMQRFHHF------------IYPNED--------PNWGTC----- 196
Cdd:pfam01266  75 ELGI------DCGFRRCGVLVLARDEEEEALEKLLAALRRLGVpaelldaeelreLEPLLPglrgglfyPDGGHVdparl 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 197 --SLEKD---------QQCPC----ENGQEPGVSTSRmccsdqCCRSLVweNCRAGWC--WEGTSWHPPG------HQAT 253
Cdd:pfam01266 149 lrALARAaealgvriiEGTEVtgieEEGGVWGVVTTG------EADAVV--NAAGAWAdlLALPGLRLPVrpvrgqVLVL 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 254 CGAKEKGPGLETPL-VADISGVYFRREGLGSNYLGGcsptEEEEPDPTNLNVDHDFFQnKVWPHLVQRVPSFKtlEVQSA 332
Cdd:pfam01266 221 EPLPEALLILPVPItVDPGRGVYLRPRADGRLLLGG----TDEEDGFDDPTPDPEEIE-ELLEAARRLFPALA--DIERA 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1039792903 333 WAGYYDynTFDQNGVVGPhPLVVNMYFATGFSGRGLQHAPGIGRAVAEI 381
Cdd:pfam01266 294 WAGLRP--LPDGLPIIGR-PGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
solA PRK11259
N-methyl-L-tryptophan oxidase;
284-400 6.21e-07

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 50.99  E-value: 6.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 284 NYLGGCSPTEEEEPDPTnlnVDHDffQNKVWPHLVQRVPSFKTLeVQSAwAGYYDyNTFDQNGVVGPHPLVVNMYFATGF 363
Cdd:PRK11259  267 NGGQEITSPDERDRFVT---VAED--GAELRPFLRNYLPGVGPC-LRGA-ACTYT-NTPDEHFIIDTLPGHPNVLVASGC 338

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039792903 364 SGRGLQHAPGIGRAVAEIMLEGHFKtIDMSPFLFTRF 400
Cdd:PRK11259  339 SGHGFKFASVLGEILADLAQDGTSD-FDLSPFSLSRF 374
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
 340-400 7.53e-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: 7.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039792903 340 NTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHfKTIDMSPFLFTRF 400
Cdd:TIGR01377 315 NTPDEHFVIDLHPKYDNVVIGAGFSGHGFKLAPVVGKILAELAMKLK-PSYDLAIFSLNRF 374
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 64-98 8.83e-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: 8.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1039792903  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];
62-399 1.06e-33

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 129.25  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903  62 EQADVVIIGGGILGLSVAFWLkkleSRRGAiRVLVVEQDHTYSRASSTgpSVGGIWQQFS---VPENVQLSLFSINFLRn 138
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHL----ARRGL-DVTVLERGRPGSGASGR--NAGQLRPGLAalaDRALVRLAREALDLWR- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 139 ineylAVVDAPPVELQFNPSGCLLLA-SEKDAATLENNVKMQRFHHfiYPNEdpnwgtcSLEKDQQCpcenGQEPGVSTS 217
Cdd:COG0665    73 -----ELAAELGIDCDFRRTGVLYLArTEAELAALRAEAEALRALG--LPVE-------LLDAAELR----EREPGLGSP 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 218 R-----------MCCSDQCCRSL----------VWENCRAgwcwegTSWHPPGHQAT-----------------CGA--- 256
Cdd:COG0665   135 DyagglydpddgHVDPAKLVRALaraaraagvrIREGTPV------TGLEREGGRVTgvrtergtvradavvlaAGAwsa 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 257 ----------------------KEKGPGLETPLVADiSGVYFRREGLGSNYLGGcspteEEEPDPTNLNVDHDFFQnKVW 314
Cdd:COG0665   209 rllpmlglrlplrpvrgyvlvtEPLPDLPLRPVLDD-TGVYLRPTADGRLLVGG-----TAEPAGFDRAPTPERLE-ALL 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 315 PHLVQRVPSFKTLEVQSAWAGYYDYnTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHfKTIDMSP 394
Cdd:COG0665   282 RRLRRLFPALADAEIVRAWAGLRPM-TPDGLPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGE-PPLDLAP 359


                  ....*
gi 1039792903 395 FLFTR 399
Cdd:COG0665   360 FSPDR 364
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 65-381 1.59e-23

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: 100.55  E-value: 1.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903  65 DVVIIGGGILGLSVAFWLkkleSRRGaIRVLVVEQDHTYSRASSTGPSvGGIWQQFSVPEN---VQLSLFSINFLRNINE 141
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYEL----ARRG-LSVTLLERGDDPGSGASGRNA-GLIHPGLRYLEPselARLALEALDLWEELEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 142 YLAVvdappvELQFNPSGCLLLASEKDAATLENNVKMQRFHHF------------IYPNED--------PNWGTC----- 196
Cdd:pfam01266  75 ELGI------DCGFRRCGVLVLARDEEEEALEKLLAALRRLGVpaelldaeelreLEPLLPglrgglfyPDGGHVdparl 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 197 --SLEKD---------QQCPC----ENGQEPGVSTSRmccsdqCCRSLVweNCRAGWC--WEGTSWHPPG------HQAT 253
Cdd:pfam01266 149 lrALARAaealgvriiEGTEVtgieEEGGVWGVVTTG------EADAVV--NAAGAWAdlLALPGLRLPVrpvrgqVLVL 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 254 CGAKEKGPGLETPL-VADISGVYFRREGLGSNYLGGcsptEEEEPDPTNLNVDHDFFQnKVWPHLVQRVPSFKtlEVQSA 332
Cdd:pfam01266 221 EPLPEALLILPVPItVDPGRGVYLRPRADGRLLLGG----TDEEDGFDDPTPDPEEIE-ELLEAARRLFPALA--DIERA 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1039792903 333 WAGYYDynTFDQNGVVGPhPLVVNMYFATGFSGRGLQHAPGIGRAVAEI 381
Cdd:pfam01266 294 WAGLRP--LPDGLPIIGR-PGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
solA PRK11259
N-methyl-L-tryptophan oxidase;
284-400 6.21e-07

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 50.99  E-value: 6.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903 284 NYLGGCSPTEEEEPDPTnlnVDHDffQNKVWPHLVQRVPSFKTLeVQSAwAGYYDyNTFDQNGVVGPHPLVVNMYFATGF 363
Cdd:PRK11259  267 NGGQEITSPDERDRFVT---VAED--GAELRPFLRNYLPGVGPC-LRGA-ACTYT-NTPDEHFIIDTLPGHPNVLVASGC 338

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039792903 364 SGRGLQHAPGIGRAVAEIMLEGHFKtIDMSPFLFTRF 400
Cdd:PRK11259  339 SGHGFKFASVLGEILADLAQDGTSD-FDLSPFSLSRF 374
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
62-99 1.58e-06

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 49.76  E-value: 1.58e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1039792903  62 EQADVVIIGGGILGLSVAFWLKKLESRrgaiRVLVVEQ 99
Cdd:COG0579     3 EMYDVVIIGAGIVGLALARELSRYEDL----KVLVLEK 36
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 63-116 1.61e-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: 1.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039792903  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 3.30e-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: 3.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039792903  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 4.06e-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: 4.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039792903  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 ...
 340-400 7.53e-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: 7.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039792903 340 NTFDQNGVVGPHPLVVNMYFATGFSGRGLQHAPGIGRAVAEIMLEGHfKTIDMSPFLFTRF 400
Cdd:TIGR01377 315 NTPDEHFVIDLHPKYDNVVIGAGFSGHGFKLAPVVGKILAELAMKLK-PSYDLAIFSLNRF 374
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
65-98 2.22e-04

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 43.27  E-value: 2.22e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1039792903  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 3.57e-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: 3.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039792903  65 DVVIIGGGILGLSVAfwlkkLESRRGAIRVLVVEQdhTYSRASSTGPSVGGIW 117
Cdd:pfam00890   1 DVLVIGGGLAGLAAA-----LAAAEAGLKVAVVEK--GQPFGGATAWSSGGID 46
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 62-116 5.52e-04

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 42.27  E-value: 5.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039792903  62 EQADVVIIGGGILGLSVAfwlkkLESRRGAIRVLVVEQDHTysRASSTGPSVGGI 116
Cdd:PRK07804   15 DAADVVVVGSGVAGLTAA-----LAARRAGRRVLVVTKAAL--DDGSTRWAQGGI 62
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 62-117 5.86e-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: 5.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039792903  62 EQADVVIIGGGILGLSVAfwlkkLESRRGAIRVLVVEQDHTY---SRASStgpsvGGIW 117
Cdd:COG1053     2 HEYDVVVVGSGGAGLRAA-----LEAAEAGLKVLVLEKVPPRgghTAAAQ-----GGIN 50
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 66-101 6.73e-04

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 41.76  E-value: 6.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1039792903  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 2.02e-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: 2.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1039792903  64 ADVVIIGGGILGLSVAFWLKKlESRRGAIRVLVVEQD 100
Cdd:TIGR00562   3 KHVVIIGGGISGLCAAYYLEK-EIPELPVELTLVEAS 38
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 17-173 4.57e-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: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903  17 RGLRtrKGGFTLdwdAKVSDFKKKVDsILPGKKYEVLYDTSHLP-------PEQADVVIIGGGILGLSVAFWLkkleSRR 89
Cdd:PRK01747  213 RGLQ--EAGFTV---RKVKGFGRKRE-MLVGELEQTLPAPLAAPwfarpgsPKARDAAIIGGGIAGAALALAL----ARR 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792903  90 GAiRVLVVEQDHTYSRASStGPSVGGIWQQFSVPENVqLSLFSIN-FLRNINEYLAVVDApPVELQFNPSGCLLLA-SEK 167
Cdd:PRK01747  283 GW-QVTLYEADEAPAQGAS-GNRQGALYPLLSKDDNA-LSRFFRAaFLFARRFYDALPAA-GVAFDHDWCGVLQLAwDEK 358


                  ....*.
gi 1039792903 168 DAATLE 173
Cdd:PRK01747  359 SAEKIA 364
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
56-106 4.57e-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: 4.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039792903  56 TSHLPPEQADVVIIGGGILGLSVAFWLkkleSRRGaIRVLVVEQDHT---YSRA 106
Cdd:PRK06183    3 AQHPDAHDTDVVIVGAGPVGLTLANLL----GQYG-VRVLVLERWPTlydLPRA 51
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 65-99 8.03e-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: 8.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1039792903  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 8.83e-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: 8.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1039792903  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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