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Conserved domains on  [gi|1424537279|ref|WP_112650026|]
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FAD-binding oxidoreductase [Mycobacterium xenopi]

Protein Classification

FAD-binding oxidoreductase( domain architecture ID 11416043)

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

EC:  1.-.-.-
Gene Ontology:  GO:0071949|GO:0016491

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
51-526 1.61e-110

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


:

Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 336.48  E-value: 1.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279  51 QADYDALAAIVgPDFCRVGDRDRLLHAggkstldllRRKDTGVQEAPDAVLLPGDEDDVAAILRHCSQRGIAVVPFGGGT 130
Cdd:COG0277     4 AALLAALRAIL-AGRVLTDPADRAAYA---------RDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 131 SVVGGLDPIRGrfdaVVSLDLRRFNRLHALDAMSGVAELGAGVTGPQAESLLGEHGFSLGHFPQSFEFATIGGFAATRSS 210
Cdd:COG0277    74 GLAGGAVPLDG----GVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 211 GQDSAGYGRFDDMVRGLRVITPAGALE--LGRAPASAAGPDLRELMIGSEGVFGVITRVRLRVHRIPEATIYEAWSFPDF 288
Cdd:COG0277   150 GPRSLKYGLTRDNVLGLEVVLADGEVVrtGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 289 ATGTAALRAVSQTGTGPTVIRLSDEAETGVNLATTEAigQQQITGGCLAITVFEGTTA-HAESRHAETRTLLEAHGGTSL 367
Cdd:COG0277   230 EAAAAAVRALLAAGIAPAALELMDRAALALVEAAPPL--GLPEDGGALLLVEFDGDDAeEVEAQLARLRAILEAGGATDV 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 368 -----GEEPAQAWQRGRFSAPYLRDsllAAGALCETLETATDWSNItalkAAVTDALTGALAASGTPAlvlCHISHVypT 442
Cdd:COG0277   308 rvaadGAERERLWKARKAALPALGR---LDGGAKLLEDVAVPPSRL----PELLRELGALAAKYGLRA---TAFGHA--G 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 443 GASLYFTVVAGQRGN-PIEQWRVAKVAACDAIMRTGGTITHHHAVGADHRPWLRDEIGELGVQILRAVKSTLDPAGILNP 521
Cdd:COG0277   376 DGNLHVRILFDPADPeEVERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNP 455

                  ....*
gi 1424537279 522 GKLIP 526
Cdd:COG0277   456 GKILP 460
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
51-526 1.61e-110

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 336.48  E-value: 1.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279  51 QADYDALAAIVgPDFCRVGDRDRLLHAggkstldllRRKDTGVQEAPDAVLLPGDEDDVAAILRHCSQRGIAVVPFGGGT 130
Cdd:COG0277     4 AALLAALRAIL-AGRVLTDPADRAAYA---------RDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 131 SVVGGLDPIRGrfdaVVSLDLRRFNRLHALDAMSGVAELGAGVTGPQAESLLGEHGFSLGHFPQSFEFATIGGFAATRSS 210
Cdd:COG0277    74 GLAGGAVPLDG----GVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 211 GQDSAGYGRFDDMVRGLRVITPAGALE--LGRAPASAAGPDLRELMIGSEGVFGVITRVRLRVHRIPEATIYEAWSFPDF 288
Cdd:COG0277   150 GPRSLKYGLTRDNVLGLEVVLADGEVVrtGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 289 ATGTAALRAVSQTGTGPTVIRLSDEAETGVNLATTEAigQQQITGGCLAITVFEGTTA-HAESRHAETRTLLEAHGGTSL 367
Cdd:COG0277   230 EAAAAAVRALLAAGIAPAALELMDRAALALVEAAPPL--GLPEDGGALLLVEFDGDDAeEVEAQLARLRAILEAGGATDV 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 368 -----GEEPAQAWQRGRFSAPYLRDsllAAGALCETLETATDWSNItalkAAVTDALTGALAASGTPAlvlCHISHVypT 442
Cdd:COG0277   308 rvaadGAERERLWKARKAALPALGR---LDGGAKLLEDVAVPPSRL----PELLRELGALAAKYGLRA---TAFGHA--G 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 443 GASLYFTVVAGQRGN-PIEQWRVAKVAACDAIMRTGGTITHHHAVGADHRPWLRDEIGELGVQILRAVKSTLDPAGILNP 521
Cdd:COG0277   376 DGNLHVRILFDPADPeEVERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNP 455

                  ....*
gi 1424537279 522 GKLIP 526
Cdd:COG0277   456 GKILP 460
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
274-524 6.58e-42

FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.


Pssm-ID: 397178  Cd Length: 248  Bit Score: 150.54  E-value: 6.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 274 IPEATIYEAWSFPDFATGTAALRAVSQTGTGPTVIRLSDEAETGVNLATTEAIGQQQITGGCLAITVFEGTT-AHAESRH 352
Cdd:pfam02913   1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFPKGLPRDAAALLLVEFEGDDeETAEEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 353 AETRTLLEAHGGTSL----GEEPAQAWQRGRFSAPYLRDSLLAAGALCETLETATDWSNItalkAAVTDALTGALAASGt 428
Cdd:pfam02913  81 EAVEAILEAGGAGDVvvatDEAEAERLWAARKYALPLRDALGGAGPAVFSEDVSVPRSRL----ADLVRDIKELLDKYG- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 429 paLVLCHISHVYPTGASLYFTVVAGQRGNPIeqwRVAKVAA--CDAIMRTGGTITHHHAVGADHRPWLRDEIGELGVQIL 506
Cdd:pfam02913 156 --LVVCLFGHAGDGNLHLYILFDFRDPEQEE---RAEKLFDeiMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALM 230
                         250
                  ....*....|....*...
gi 1424537279 507 RAVKSTLDPAGILNPGKL 524
Cdd:pfam02913 231 RRIKAAFDPKGILNPGKV 248
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
97-526 8.28e-42

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 157.48  E-value: 8.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279  97 PDAVLLPGDEDDVAAILRHCSQRGIAVVPFGGGTSVVG-GLDPIRGrfdavVSLDLRRFNRLHAL--DAMSGVAELGAGV 173
Cdd:PLN02805  134 PDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGhTLAPHGG-----VCIDMSLMKSVKALhvEDMDVVVEPGIGW 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 174 TgpQAESLLGEHG--FSLGHFPQsfefATIGGFAATRSSGQDSAGYGRFDDMVRGLRVITPAGAL--ELGRAPASAAGPD 249
Cdd:PLN02805  209 L--ELNEYLEPYGlfFPLDPGPG----ATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVvkTASRARKSAAGYD 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 250 LRELMIGSEGVFGVITRVRLRVHRIPEATIYEAWSFPDFATGTAALRAVSQTGTGPTVIRLSDEAET-GVNLATTEAIGQ 328
Cdd:PLN02805  283 LTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIATMLSGIQVSRVELLDEVQIrAINMANGKNLPE 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 329 qqitggcLAITVFE--GTTAHAESRHAETRTLLEAHGGTS--LGEEP---AQAWQrgrfsapYLRDSLLAAGALCETLET 401
Cdd:PLN02805  363 -------APTLMFEfiGTEAYAREQTLIVQKIASKHNGSDfvFAEEPeakKELWK-------IRKEALWACFAMEPKYEA 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 402 A-TDWSNITALKAAVTDALTGALAASGTPALVLCHishvypTGASLYFTVVAGQRGNPIEQWRVAKVA--ACDAIMRTGG 478
Cdd:PLN02805  429 MiTDVCVPLSHLAELISRSKKELDASPLVCTVIAH------AGDGNFHTIILFDPSQEDQRREAERLNhfMVHTALSMEG 502
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1424537279 479 TITHHHAVGADHRPWLRDEIGELGVQILRAVKSTLDPAGILNPGKLIP 526
Cdd:PLN02805  503 TCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIP 550
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
99-269 2.03e-05

plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.


Pssm-ID: 273750 [Multi-domain]  Cd Length: 557  Bit Score: 47.16  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279  99 AVLLPGDEDDVAAILRHCSQRGIAVVPFGGGTSVVGGLDPIRGRfDAVVSLDLRRFNRLHALDAMSGVAELGAGVTGPQA 178
Cdd:TIGR01677  34 NVAYPKTEAELVSVVAAATAAGRKMKVVTRYSHSIPKLACPDGS-DGALLISTKRLNHVVAVDATAMTVTVESGMSLREL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 179 ESLLGEHGFSLGHFPQsFEFATIGGFAATRSSGQDSAGYG-RFDDMVRGLRVITPAGALE-LGRAPASAAGPDLRELMIG 256
Cdd:TIGR01677 113 IVEAEKAGLALPYAPY-WWGLTVGGMMGTGAHGSSLWGKGsAVHDYVVGIRLVVPASAAEgFAKVRILSEGDTPNEFNAA 191
                         170
                  ....*....|....*
gi 1424537279 257 --SEGVFGVITRVRL 269
Cdd:TIGR01677 192 kvSLGVLGVISQVTL 206
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
51-526 1.61e-110

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 336.48  E-value: 1.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279  51 QADYDALAAIVgPDFCRVGDRDRLLHAggkstldllRRKDTGVQEAPDAVLLPGDEDDVAAILRHCSQRGIAVVPFGGGT 130
Cdd:COG0277     4 AALLAALRAIL-AGRVLTDPADRAAYA---------RDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 131 SVVGGLDPIRGrfdaVVSLDLRRFNRLHALDAMSGVAELGAGVTGPQAESLLGEHGFSLGHFPQSFEFATIGGFAATRSS 210
Cdd:COG0277    74 GLAGGAVPLDG----GVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 211 GQDSAGYGRFDDMVRGLRVITPAGALE--LGRAPASAAGPDLRELMIGSEGVFGVITRVRLRVHRIPEATIYEAWSFPDF 288
Cdd:COG0277   150 GPRSLKYGLTRDNVLGLEVVLADGEVVrtGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 289 ATGTAALRAVSQTGTGPTVIRLSDEAETGVNLATTEAigQQQITGGCLAITVFEGTTA-HAESRHAETRTLLEAHGGTSL 367
Cdd:COG0277   230 EAAAAAVRALLAAGIAPAALELMDRAALALVEAAPPL--GLPEDGGALLLVEFDGDDAeEVEAQLARLRAILEAGGATDV 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 368 -----GEEPAQAWQRGRFSAPYLRDsllAAGALCETLETATDWSNItalkAAVTDALTGALAASGTPAlvlCHISHVypT 442
Cdd:COG0277   308 rvaadGAERERLWKARKAALPALGR---LDGGAKLLEDVAVPPSRL----PELLRELGALAAKYGLRA---TAFGHA--G 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 443 GASLYFTVVAGQRGN-PIEQWRVAKVAACDAIMRTGGTITHHHAVGADHRPWLRDEIGELGVQILRAVKSTLDPAGILNP 521
Cdd:COG0277   376 DGNLHVRILFDPADPeEVERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNP 455

                  ....*
gi 1424537279 522 GKLIP 526
Cdd:COG0277   456 GKILP 460
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
274-524 6.58e-42

FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.


Pssm-ID: 397178  Cd Length: 248  Bit Score: 150.54  E-value: 6.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 274 IPEATIYEAWSFPDFATGTAALRAVSQTGTGPTVIRLSDEAETGVNLATTEAIGQQQITGGCLAITVFEGTT-AHAESRH 352
Cdd:pfam02913   1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFPKGLPRDAAALLLVEFEGDDeETAEEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 353 AETRTLLEAHGGTSL----GEEPAQAWQRGRFSAPYLRDSLLAAGALCETLETATDWSNItalkAAVTDALTGALAASGt 428
Cdd:pfam02913  81 EAVEAILEAGGAGDVvvatDEAEAERLWAARKYALPLRDALGGAGPAVFSEDVSVPRSRL----ADLVRDIKELLDKYG- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 429 paLVLCHISHVYPTGASLYFTVVAGQRGNPIeqwRVAKVAA--CDAIMRTGGTITHHHAVGADHRPWLRDEIGELGVQIL 506
Cdd:pfam02913 156 --LVVCLFGHAGDGNLHLYILFDFRDPEQEE---RAEKLFDeiMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALM 230
                         250
                  ....*....|....*...
gi 1424537279 507 RAVKSTLDPAGILNPGKL 524
Cdd:pfam02913 231 RRIKAAFDPKGILNPGKV 248
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
97-526 8.28e-42

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 157.48  E-value: 8.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279  97 PDAVLLPGDEDDVAAILRHCSQRGIAVVPFGGGTSVVG-GLDPIRGrfdavVSLDLRRFNRLHAL--DAMSGVAELGAGV 173
Cdd:PLN02805  134 PDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGhTLAPHGG-----VCIDMSLMKSVKALhvEDMDVVVEPGIGW 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 174 TgpQAESLLGEHG--FSLGHFPQsfefATIGGFAATRSSGQDSAGYGRFDDMVRGLRVITPAGAL--ELGRAPASAAGPD 249
Cdd:PLN02805  209 L--ELNEYLEPYGlfFPLDPGPG----ATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVvkTASRARKSAAGYD 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 250 LRELMIGSEGVFGVITRVRLRVHRIPEATIYEAWSFPDFATGTAALRAVSQTGTGPTVIRLSDEAET-GVNLATTEAIGQ 328
Cdd:PLN02805  283 LTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIATMLSGIQVSRVELLDEVQIrAINMANGKNLPE 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 329 qqitggcLAITVFE--GTTAHAESRHAETRTLLEAHGGTS--LGEEP---AQAWQrgrfsapYLRDSLLAAGALCETLET 401
Cdd:PLN02805  363 -------APTLMFEfiGTEAYAREQTLIVQKIASKHNGSDfvFAEEPeakKELWK-------IRKEALWACFAMEPKYEA 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 402 A-TDWSNITALKAAVTDALTGALAASGTPALVLCHishvypTGASLYFTVVAGQRGNPIEQWRVAKVA--ACDAIMRTGG 478
Cdd:PLN02805  429 MiTDVCVPLSHLAELISRSKKELDASPLVCTVIAH------AGDGNFHTIILFDPSQEDQRREAERLNhfMVHTALSMEG 502
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1424537279 479 TITHHHAVGADHRPWLRDEIGELGVQILRAVKSTLDPAGILNPGKLIP 526
Cdd:PLN02805  503 TCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIP 550
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
97-234 8.89e-37

FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 426326 [Multi-domain]  Cd Length: 139  Bit Score: 132.71  E-value: 8.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279  97 PDAVLLPGDEDDVAAILRHCSQRGIAVVPFGGGTSVVGGldpiRGRFDAVVsLDLRRFNRLHALDAMSGVAELGAGVTGP 176
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGG----AVQTGGIV-LDLSRLNGILEIDPEDGTATVEAGVTLG 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1424537279 177 QAESLLGEHGFSLGHFPQSFEFATIGGFAATRSSGQDSAGYGRFDDMVRGLRVITPAG 234
Cdd:pfam01565  76 DLVRALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADG 133
PRK11230 PRK11230
glycolate oxidase subunit GlcD; Provisional
97-526 1.15e-17

glycolate oxidase subunit GlcD; Provisional


Pssm-ID: 183043 [Multi-domain]  Cd Length: 499  Bit Score: 85.60  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279  97 PDAVLLPGDEDDVAAILRHCSQRGIAVVPFGGGTSVVGGLDPIrgrfDAVVSLDLRRFNRLHALDAMSGVAELGAGVTGP 176
Cdd:PRK11230   56 PLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPL----EKGVLLVMARFNRILDINPVGRRARVQPGVRNL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 177 QAESLLGEHGFSLGHFPQSFEFATIGGFAATRSSGQDSAGYGRFDDMVRGLRVITPAG-ALELGRAPASAAGPDLRELMI 255
Cdd:PRK11230  132 AISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGeALTLGSDALDSPGFDLLALFT 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 256 GSEGVFGVITRVRLRVHRIPEATIYEAWSFPDFATGTAALRAVSQTGTGPTVIRLSDeaetgvNLATTEAigQQQITGG- 334
Cdd:PRK11230  212 GSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPGGLEMMD------NLSIRAA--EDFIHAGy 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 335 ---CLAITVFE--GTTAHAESRHAETRTLLEAHGGTSLGEEPAQAwQRGRFSAPYlRDSLLAAGALcetletATDWSNI- 408
Cdd:PRK11230  284 pvdAEAILLCEldGVESDVQEDCERVNDILLKAGATDVRLAQDEA-ERVRFWAGR-KNAFPAVGRI------SPDYYCMd 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 409 -TALKAAVTDALTGALAASGTPALvlcHISHVYPTGASLYFTVVAGQRGNPIEQWRVAKVAA-----CDAImrtGGTITH 482
Cdd:PRK11230  356 gTIPRRELPGVLEGIARLSQQYGL---RVANVFHAGDGNMHPLILFDANEPGELERAEALGGkilelCVEV---GGSITG 429
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1424537279 483 HHAVGadhrpwlRDEIGELGVQ-------ILRAVKSTLDPAGILNPGKLIP 526
Cdd:PRK11230  430 EHGVG-------REKINQMCAQfnsdeitLFHAVKAAFDPDGLLNPGKNIP 473
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
99-269 2.03e-05

plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.


Pssm-ID: 273750 [Multi-domain]  Cd Length: 557  Bit Score: 47.16  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279  99 AVLLPGDEDDVAAILRHCSQRGIAVVPFGGGTSVVGGLDPIRGRfDAVVSLDLRRFNRLHALDAMSGVAELGAGVTGPQA 178
Cdd:TIGR01677  34 NVAYPKTEAELVSVVAAATAAGRKMKVVTRYSHSIPKLACPDGS-DGALLISTKRLNHVVAVDATAMTVTVESGMSLREL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 179 ESLLGEHGFSLGHFPQsFEFATIGGFAATRSSGQDSAGYG-RFDDMVRGLRVITPAGALE-LGRAPASAAGPDLRELMIG 256
Cdd:TIGR01677 113 IVEAEKAGLALPYAPY-WWGLTVGGMMGTGAHGSSLWGKGsAVHDYVVGIRLVVPASAAEgFAKVRILSEGDTPNEFNAA 191
                         170
                  ....*....|....*
gi 1424537279 257 --SEGVFGVITRVRL 269
Cdd:TIGR01677 192 kvSLGVLGVISQVTL 206
glcE PRK11282
glycolate oxidase FAD binding subunit; Provisional
179-279 7.84e-04

glycolate oxidase FAD binding subunit; Provisional


Pssm-ID: 236893 [Multi-domain]  Cd Length: 352  Bit Score: 41.75  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424537279 179 ESLLGEHGFSLGHFPQSF-EFATIGGFAATRSSG--QDSAGYGRfdDMVRGLRVITPAGALeL---GRAPASAAGPDLRE 252
Cdd:PRK11282   71 EAALAEAGQMLPFEPPHFgGGATLGGMVAAGLSGprRPWAGAVR--DFVLGTRLINGRGEH-LrfgGQVMKNVAGYDVSR 147
                          90       100
                  ....*....|....*....|....*..
gi 1424537279 253 LMIGSEGVFGVITRVRLRVHRIPEATI 279
Cdd:PRK11282  148 LMAGSLGTLGVLLEVSLKVLPRPRAEL 174
 
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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