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Conserved domains on  [gi|446967497|ref|WP_001044753|]
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MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Bacillus]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11428914)

NAD(P)/FAD-dependent oxidoreductase similar to digeranylgeranylglycerophospholipid reductase, menaquinone reductase, tryptophan 2-halogenase, and protein FixC

EC:  1.-.-.-
Gene Ontology:  GO:0000166|GO:0071949|GO:0016491
PubMed:  30945211
SCOP:  3000055

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
15-346 9.52e-39

Dehydrogenase (flavoprotein) [Energy production and conversion];


:

Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 140.49  E-value: 9.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  15 AGSTLAIYLAKAGFHVLLVDRANFPRDTLSTHTFFNNTVALLRETGVLDKLletkAPPVRDIKFQFEDTVIEGLIPevyG 94
Cdd:COG0644    4 AGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPL----ERPVRGARFYSPGGKSVELPP---G 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  95 EESCYCIRRTYLDHILLEQAKsQMNVTVLEGFRVTDVIRDDETVIgVKGLDGdnekQEFLARLVVGADGRSSIIRKLVKS 174
Cdd:COG0644   77 RGGGYVVDRARFDRWLAEQAE-EAGAEVRTGTRVTDVLRDDGRVV-VRTGDG----EEIRADYVVDADGARSLLARKLGL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 175 ELKISIPATVGI-YFGYFSGFRHDNVPKFEVYKIKDNTAI-----LFPTNDDLyVIVGIfplenkelierlklnPESCLR 248
Cdd:COG0644  151 KRRSDEPQDYALaIKEHWELPPLEGVDPGAVEFFFGEGAPggygwVFPLGDGR-VSVGI---------------PLGGPR 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 249 NFFTdnfpnttigarlknaelvepakgilgydnywykgmGKGWALVGDAVCFKDPGMAQGIHDAICGARILSNILSKYKG 328
Cdd:COG0644  215 PRLV-----------------------------------GDGVLLVGDAAGFVDPLTGEGIHLAMKSGRLAAEAIAEALE 259
                        330
                 ....*....|....*...
gi 446967497 329 QSDQSNQMSEEYQKAIED 346
Cdd:COG0644  260 GGDFSAEALAEYERRLRE 277
 
Name Accession Description Interval E-value
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
15-346 9.52e-39

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 140.49  E-value: 9.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  15 AGSTLAIYLAKAGFHVLLVDRANFPRDTLSTHTFFNNTVALLRETGVLDKLletkAPPVRDIKFQFEDTVIEGLIPevyG 94
Cdd:COG0644    4 AGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPL----ERPVRGARFYSPGGKSVELPP---G 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  95 EESCYCIRRTYLDHILLEQAKsQMNVTVLEGFRVTDVIRDDETVIgVKGLDGdnekQEFLARLVVGADGRSSIIRKLVKS 174
Cdd:COG0644   77 RGGGYVVDRARFDRWLAEQAE-EAGAEVRTGTRVTDVLRDDGRVV-VRTGDG----EEIRADYVVDADGARSLLARKLGL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 175 ELKISIPATVGI-YFGYFSGFRHDNVPKFEVYKIKDNTAI-----LFPTNDDLyVIVGIfplenkelierlklnPESCLR 248
Cdd:COG0644  151 KRRSDEPQDYALaIKEHWELPPLEGVDPGAVEFFFGEGAPggygwVFPLGDGR-VSVGI---------------PLGGPR 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 249 NFFTdnfpnttigarlknaelvepakgilgydnywykgmGKGWALVGDAVCFKDPGMAQGIHDAICGARILSNILSKYKG 328
Cdd:COG0644  215 PRLV-----------------------------------GDGVLLVGDAAGFVDPLTGEGIHLAMKSGRLAAEAIAEALE 259
                        330
                 ....*....|....*...
gi 446967497 329 QSDQSNQMSEEYQKAIED 346
Cdd:COG0644  260 GGDFSAEALAEYERRLRE 277
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
5-318 4.93e-26

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 106.63  E-value: 4.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497    5 YDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFPR-----DTLSthtffnntvallreTGVLDKLLETKAPPVRDIK-- 77
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRykpcgGALS--------------PRALEELDLPGELIVNLVRga 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   78 ---FQFEDTViEGLIPEVYGeescYCIRRTYLDHILLEQAKSQmNVTVLEGFRVTDV-IRDDETVIGVKGldgdnEKQEF 153
Cdd:TIGR02032  67 rffSPNGDSV-EIPIETELA----YVIDRDAFDEQLAERAQEA-GAELRLGTRVLDVeIHDDRVVVIVRG-----SEGTV 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  154 LARLVVGADGRSSIIRKLV---------KSELKISIPATVGIYfgyfsgfRHDNVpkfEVYKIKDNT----AILFPTNDD 220
Cdd:TIGR02032 136 TAKIVIGADGSRSIVAKKLglkkepreyGVAARAEVEMPDEEV-------DEDFV---EVYIDRGIVpggyGWVFPKGDG 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  221 LY-VIVGIFPLENKE-LIERLKlnpesclrnFFTDNFPnttigaRLKNAELVEPAKGILGYDNYWYKGMGKGWALVGDAV 298
Cdd:TIGR02032 206 TAnVGVGSRSAEEGEdPKKYLK---------DFLARRP------ELKDAETVEVCGALIPIGRPDEKLVRGNVLLVGDAA 270
                         330       340
                  ....*....|....*....|
gi 446967497  299 CFKDPGMAQGIHDAICGARI 318
Cdd:TIGR02032 271 GHVNPLTGEGIYYAMRSGDI 290
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
5-239 6.11e-19

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 87.38  E-value: 6.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497    5 YDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFPRDTLSTHTFFNNTVALLRETGVLDKLLETKAPPVRdikfqFEDTV 84
Cdd:pfam01494   2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPRAHGLNQRTMELLRQAGLEDRILAEGVPHEG-----MGLAF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   85 IEGLIPEVYGEESCYC----IRRTYLDHILLEQAkSQMNVTVLEGFRVTDVIRDDETVIGVKGLDGDNEKQEFLARLVVG 160
Cdd:pfam01494  77 YNTRRRADLDFLTSPPrvtvYPQTELEPILVEHA-EARGAQVRFGTEVLSLEQDGDGVTAVVRDRRDGEEYTVRAKYLVG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  161 ADGRSSIIRKlvksELKISIPATVGIYFGYFS-GFRHDNVPKFEvykiKDNTAILFPTNDDlYVIVGIFPLENKELIERL 239
Cdd:pfam01494 156 CDGGRSPVRK----TLGIEFEGFEGVPFGSLDvLFDAPDLSDPV----ERAFVHYLIYAPH-SRGFMVGPWRSAGRERYY 226
PRK06185 PRK06185
FAD-dependent oxidoreductase;
1-171 3.65e-15

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 76.44  E-value: 3.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   1 MNKTYDVIITGARCAGSTLAIYLAKAGFHVLLVDR-ANFPRD----TLSThtffnNTVALLRETGVLDKLLETKAPPVRD 75
Cdd:PRK06185   3 EVETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEKhADFLRDfrgdTVHP-----STLELMDELGLLERFLELPHQKVRT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  76 IKFqfedtvieglipEVYGEEscycIRRTYLDHI------------------LLEQAKSQMNVTVLEGFRVTDVIRDDET 137
Cdd:PRK06185  78 LRF------------EIGGRT----VTLADFSRLptpypyiammpqwdfldfLAEEASAYPNFTLRMGAEVTGLIEEGGR 141
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446967497 138 VIGVKGLDGDNEkQEFLARLVVGADGRSSIIRKL 171
Cdd:PRK06185 142 VTGVRARTPDGP-GEIRADLVVGADGRHSRVRAL 174
 
Name Accession Description Interval E-value
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
15-346 9.52e-39

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 140.49  E-value: 9.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  15 AGSTLAIYLAKAGFHVLLVDRANFPRDTLSTHTFFNNTVALLRETGVLDKLletkAPPVRDIKFQFEDTVIEGLIPevyG 94
Cdd:COG0644    4 AGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPL----ERPVRGARFYSPGGKSVELPP---G 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  95 EESCYCIRRTYLDHILLEQAKsQMNVTVLEGFRVTDVIRDDETVIgVKGLDGdnekQEFLARLVVGADGRSSIIRKLVKS 174
Cdd:COG0644   77 RGGGYVVDRARFDRWLAEQAE-EAGAEVRTGTRVTDVLRDDGRVV-VRTGDG----EEIRADYVVDADGARSLLARKLGL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 175 ELKISIPATVGI-YFGYFSGFRHDNVPKFEVYKIKDNTAI-----LFPTNDDLyVIVGIfplenkelierlklnPESCLR 248
Cdd:COG0644  151 KRRSDEPQDYALaIKEHWELPPLEGVDPGAVEFFFGEGAPggygwVFPLGDGR-VSVGI---------------PLGGPR 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 249 NFFTdnfpnttigarlknaelvepakgilgydnywykgmGKGWALVGDAVCFKDPGMAQGIHDAICGARILSNILSKYKG 328
Cdd:COG0644  215 PRLV-----------------------------------GDGVLLVGDAAGFVDPLTGEGIHLAMKSGRLAAEAIAEALE 259
                        330
                 ....*....|....*...
gi 446967497 329 QSDQSNQMSEEYQKAIED 346
Cdd:COG0644  260 GGDFSAEALAEYERRLRE 277
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
2-172 1.07e-27

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: 111.57  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   2 NKTYDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFPRDTLSTHTFFNNTVALLRETGVLDKLLEtKAPPVRDIKFQFE 81
Cdd:COG0654    1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLA-RGAPIRGIRVRDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  82 DT--VIEGLIPEVYGEESCYCIRRTYLDHILLEQAKSQmNVTVLEGFRVTDVIRDDETViGVKGLDGdnekQEFLARLVV 159
Cdd:COG0654   80 SDgrVLARFDAAETGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGV-TVTLADG----RTLRADLVV 153
                        170
                 ....*....|...
gi 446967497 160 GADGRSSIIRKLV 172
Cdd:COG0654  154 GADGARSAVRRLL 166
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
5-318 4.93e-26

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 106.63  E-value: 4.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497    5 YDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFPR-----DTLSthtffnntvallreTGVLDKLLETKAPPVRDIK-- 77
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRykpcgGALS--------------PRALEELDLPGELIVNLVRga 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   78 ---FQFEDTViEGLIPEVYGeescYCIRRTYLDHILLEQAKSQmNVTVLEGFRVTDV-IRDDETVIGVKGldgdnEKQEF 153
Cdd:TIGR02032  67 rffSPNGDSV-EIPIETELA----YVIDRDAFDEQLAERAQEA-GAELRLGTRVLDVeIHDDRVVVIVRG-----SEGTV 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  154 LARLVVGADGRSSIIRKLV---------KSELKISIPATVGIYfgyfsgfRHDNVpkfEVYKIKDNT----AILFPTNDD 220
Cdd:TIGR02032 136 TAKIVIGADGSRSIVAKKLglkkepreyGVAARAEVEMPDEEV-------DEDFV---EVYIDRGIVpggyGWVFPKGDG 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  221 LY-VIVGIFPLENKE-LIERLKlnpesclrnFFTDNFPnttigaRLKNAELVEPAKGILGYDNYWYKGMGKGWALVGDAV 298
Cdd:TIGR02032 206 TAnVGVGSRSAEEGEdPKKYLK---------DFLARRP------ELKDAETVEVCGALIPIGRPDEKLVRGNVLLVGDAA 270
                         330       340
                  ....*....|....*....|
gi 446967497  299 CFKDPGMAQGIHDAICGARI 318
Cdd:TIGR02032 271 GHVNPLTGEGIYYAMRSGDI 290
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
5-239 6.11e-19

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 87.38  E-value: 6.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497    5 YDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFPRDTLSTHTFFNNTVALLRETGVLDKLLETKAPPVRdikfqFEDTV 84
Cdd:pfam01494   2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPRAHGLNQRTMELLRQAGLEDRILAEGVPHEG-----MGLAF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   85 IEGLIPEVYGEESCYC----IRRTYLDHILLEQAkSQMNVTVLEGFRVTDVIRDDETVIGVKGLDGDNEKQEFLARLVVG 160
Cdd:pfam01494  77 YNTRRRADLDFLTSPPrvtvYPQTELEPILVEHA-EARGAQVRFGTEVLSLEQDGDGVTAVVRDRRDGEEYTVRAKYLVG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  161 ADGRSSIIRKlvksELKISIPATVGIYFGYFS-GFRHDNVPKFEvykiKDNTAILFPTNDDlYVIVGIFPLENKELIERL 239
Cdd:pfam01494 156 CDGGRSPVRK----TLGIEFEGFEGVPFGSLDvLFDAPDLSDPV----ERAFVHYLIYAPH-SRGFMVGPWRSAGRERYY 226
PRK06185 PRK06185
FAD-dependent oxidoreductase;
1-171 3.65e-15

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 76.44  E-value: 3.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   1 MNKTYDVIITGARCAGSTLAIYLAKAGFHVLLVDR-ANFPRD----TLSThtffnNTVALLRETGVLDKLLETKAPPVRD 75
Cdd:PRK06185   3 EVETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEKhADFLRDfrgdTVHP-----STLELMDELGLLERFLELPHQKVRT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  76 IKFqfedtvieglipEVYGEEscycIRRTYLDHI------------------LLEQAKSQMNVTVLEGFRVTDVIRDDET 137
Cdd:PRK06185  78 LRF------------EIGGRT----VTLADFSRLptpypyiammpqwdfldfLAEEASAYPNFTLRMGAEVTGLIEEGGR 141
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446967497 138 VIGVKGLDGDNEkQEFLARLVVGADGRSSIIRKL 171
Cdd:PRK06185 142 VTGVRARTPDGP-GEIRADLVVGADGRHSRVRAL 174
PRK09126 PRK09126
FAD-dependent hydroxylase;
3-184 2.00e-14

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 74.21  E-value: 2.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   3 KTYDVIITGARCAGSTLAIYLAKAGFHVLLVDRAnfPRDTLS-----------THTffnnTVALLRETGVLDKLLETKAP 71
Cdd:PRK09126   2 MHSDIVVVGAGPAGLSFARSLAGSGLKVTLIERQ--PLAALAdpafdgreialTHA----SREILQRLGAWDRIPEDEIS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  72 PVRDIK-----------FQFEDTVIEGL---IPEvygeescYCIRRTyldhiLLEQAKSQMNVTVLEGFRVTDViRDDET 137
Cdd:PRK09126  76 PLRDAKvlngrspfaltFDARGRGADALgylVPN-------HLIRRA-----AYEAVSQQDGIELLTGTRVTAV-RTDDD 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446967497 138 VIGVKGLDGDNEKqeflARLVVGADGRSSIIRKlvkselKISIPATV 184
Cdd:PRK09126 143 GAQVTLANGRRLT----ARLLVAADSRFSATRR------QLGIGADM 179
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
6-171 1.67e-13

Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273913 [Multi-domain]  Cd Length: 385  Bit Score: 71.47  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497    6 DVIITGARCAGSTLAIYLAKAGFHVLLVDRANFPRdtlSTHTFFNN--------TVALLRETGVLDKLLETKAPPVRDIk 77
Cdd:TIGR01988   1 DIVIVGGGMVGLALALALARSGLKVALIEATPLPA---PADPGFDNrvsalsaaSIRLLEKLGVWDKIEPARAQPIRDI- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   78 fQFEDTVIEGLI---PEVYGEESC-YCIRRTYLDHILLEQAKSQMNVTVLEGFRVTDVIRDDETVIgVKgLDGDnekQEF 153
Cdd:TIGR01988  77 -HVSDGGSFGALrfdADEIGLEALgYVVENRVLQQALWERLQELPNVTLLCPARVVELPRHSDHVE-LT-LDDG---QQL 150
                         170
                  ....*....|....*...
gi 446967497  154 LARLVVGADGRSSIIRKL 171
Cdd:TIGR01988 151 RARLLVGADGANSKVRQL 168
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
1-170 5.70e-12

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 66.85  E-value: 5.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   1 MNKTYDVIITGARCAGSTLAIYLAKAGFHVLLVDRAnFPRDTLSTHTFFNNTVALLRETGVLDKlLETKAPPVRDIKfqf 80
Cdd:PRK07494   4 EKEHTDIAVIGGGPAGLAAAIALARAGASVALVAPE-PPYADLRTTALLGPSIRFLERLGLWAR-LAPHAAPLQSMR--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  81 edtVIEG---LI--PEVY------GEESC-YCIRRTYLDHILLEQAKSQMNVTVLEGFRVTDVIRDDETVIGVKglDGdn 148
Cdd:PRK07494  79 ---IVDAtgrLIraPEVRfraaeiGEDAFgYNIPNWLLNRALEARVAELPNITRFGDEAESVRPREDEVTVTLA--DG-- 151
                        170       180
                 ....*....|....*....|..
gi 446967497 149 ekQEFLARLVVGADGRSSIIRK 170
Cdd:PRK07494 152 --TTLSARLVVGADGRNSPVRE 171
PRK06847 PRK06847
hypothetical protein; Provisional
1-313 1.63e-10

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 62.20  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   1 MNKTYDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFPRDTLSTHTFFNNTVALLRETGVLDKLLETkappvrdiKFQF 80
Cdd:PRK06847   1 MAAVKKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYGAGITLQGNALRALRELGVLDECLEA--------GFGF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  81 EDTVI---------EGLIPEVYGEE--SCYCIRRTYLDHILLEQAKsQMNVTVLEGFRVTDVIRDDEtviGVKGLDGDNE 149
Cdd:PRK06847  73 DGVDLfdpdgtllaELPTPRLAGDDlpGGGGIMRPALARILADAAR-AAGADVRLGTTVTAIEQDDD---GVTVTFSDGT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 150 KQEFlaRLVVGADGRSSIIRKLVKSELKISIPATVGIYFGYFSgfRHDNVPKFEVYKIKDNTAILFPTNDDL-YVIVgif 228
Cdd:PRK06847 149 TGRY--DLVVGADGLYSKVRSLVFPDEPEPEYTGQGVWRAVLP--RPAEVDRSLMYLGPTTKAGVVPLSEDLmYLFV--- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 229 pLENKEliERLKLNPESCLRNF--FTDNFPNTTIGARLKNaeLVEPAK------GILGYDNYWYKGMgkgWALVGDAVCF 300
Cdd:PRK06847 222 -TEPRP--DNPRIEPDTLAALLreLLAPFGGPVLQELREQ--ITDDAQvvyrplETLLVPAPWHRGR---VVLIGDAAHA 293
                        330
                 ....*....|....*..
gi 446967497 301 KDPGMAQG----IHDAI 313
Cdd:PRK06847 294 TTPHLAQGagmaIEDAI 310
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
4-176 3.38e-09

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 58.38  E-value: 3.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   4 TYDVIITGARCAGSTLAIYLAKAGFHVLLVDRA----NFPR------------------DTLSTHTFFNNTVALLRETGV 61
Cdd:PRK06183  10 DTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWptlyDLPRavgiddealrvlqaiglaDEVLPHTTPNHGMRFLDAKGR 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  62 LdkLLETKAPPVRDikfqfedtvieglipevYGeescYCIRRTY----LDHILLEQAKSQMNVTVLEGFRVTDVIRDDET 137
Cdd:PRK06183  90 C--LAEIARPSTGE-----------------FG----WPRRNAFhqplLEAVLRAGLARFPHVRVRFGHEVTALTQDDDG 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446967497 138 V-IGVKGLDGdnEKQEFLARLVVGADGRSSIIRKLVKSEL 176
Cdd:PRK06183 147 VtVTLTDADG--QRETVRARYVVGCDGANSFVRRTLGVPF 184
PRK06126 PRK06126
hypothetical protein; Provisional
6-170 1.07e-08

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 56.93  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   6 DVIITGARCAGSTLAIYLAKAGFHVLLVDRanfpRDTLSTHTFFNNTVA----LLRETGVLDKLLETKAPP--VRDI--- 76
Cdd:PRK06126   9 PVLIVGGGPVGLALALDLGRRGVDSILVER----KDGTAFNPKANTTSArsmeHFRRLGIADEVRSAGLPVdyPTDIayf 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  77 ---------KFQF-----EDTVIEGLIPEVYGEESCYCIRRTYLDHILLEQAKSQMNVTVLEGFRVTDVIRDDETVIG-V 141
Cdd:PRK06126  85 trltgyelaRFRLpsareAITPVGGPDGSWPSPELPHRIPQKYLEPILLEHAAAQPGVTLRYGHRLTDFEQDADGVTAtV 164
                        170       180
                 ....*....|....*....|....*....
gi 446967497 142 KGLDGDnEKQEFLARLVVGADGRSSIIRK 170
Cdd:PRK06126 165 EDLDGG-ESLTIRADYLVGCDGARSAVRR 192
PRK11445 PRK11445
FAD-binding protein;
5-327 2.75e-08

FAD-binding protein;


Pssm-ID: 183139 [Multi-domain]  Cd Length: 351  Bit Score: 55.07  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   5 YDVIITGARCAGSTLAIYLAKAgFHVLLVDRanfpRDTLSTHTFFNNTVALL-----RETGVLD---------------- 63
Cdd:PRK11445   2 YDVAIIGLGPAGSALARLLAGK-MKVIAIDK----KHQCGTEGFSKPCGGLLapdaqKSFAKDGltlpkdvianpqifav 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  64 KLLETKAPPVRDI----------KFqfeDTVIEGLIP---EVYGEESCYCIRRTyldhilleqaksqmnvtvLEGFRVTd 130
Cdd:PRK11445  77 KTIDLANSLTRNYqrsyinidrhKF---DLWLKSLIPasvEVYHNSLCRKIWRE------------------DDGYHVI- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 131 virddetvigvkgLDGDNEKQEFLARLVVGADGRSSIIRKLVKSELKisIPATVGIYfGYFSgfRHDNVPKFevykikdn 210
Cdd:PRK11445 135 -------------FRADGWEQHITARYLVGADGANSMVRRHLYPDHQ--IRKYVAIQ-QWFA--EKHPVPFY-------- 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 211 TAILFPTNDDLY----------VIVGIFPLEN-KELIERLKlnpeSCLRNF-FtdNFPNTTigaRLKNAELVEPAKG--- 275
Cdd:PRK11445 189 SCIFDNEITDCYswsiskdgyfIFGGAYPMKDgRERFETLK----EKLSAFgF--QFGKPV---KTEACTVLRPSRWqdf 259
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446967497 276 ILGYDNYwykgmgkgwALVGDAVCFKDPGMAQGIHDAICGARILSNILSKYK 327
Cdd:PRK11445 260 VCGKDNA---------FLIGEAAGFISPSSLEGISYALDSARILSEVLNKQP 302
PRK10015 PRK10015
oxidoreductase; Provisional
5-168 1.64e-07

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 53.06  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   5 YDVIITGARCAGSTLAIYLAKAGFHVLLVDRA------NFPRDTLSTHTFFNNTVALLRETGVLDKLLETKappvrdIKF 78
Cdd:PRK10015   6 FDAIVVGAGVAGSVAALVMARAGLDVLVIERGdsagckNMTGGRLYAHTLEAIIPGFAASAPVERKVTREK------ISF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  79 QFEDTVI----EGLIPEVYGEEScYCIRRTYLDHILLEQAKsQMNVTVLEGFRVTDVIRDDETVIGVKGldGDNEKQefl 154
Cdd:PRK10015  80 LTEESAVtldfHREQPDVPQHAS-YTVLRNRLDPWLMEQAE-QAGAQFIPGVRVDALVREGNKVTGVQA--GDDILE--- 152
                        170
                 ....*....|....
gi 446967497 155 ARLVVGADGRSSII 168
Cdd:PRK10015 153 ANVVILADGVNSML 166
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
5-168 2.83e-07

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 52.22  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   5 YDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFP--RDTLSTHTFFNNTVALLREtgvldklLETKAPPVRDI---KFQ 79
Cdd:PRK10157   6 FDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAgaKNVTGGRLYAHSLEHIIPG-------FADSAPVERLItheKLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  80 FEDTVIEGLIPEVYGEESC-----YCIRRTYLDHILLEQAKsQMNVTVLEGFRVTDVIRDDETVIGVKGlDGDNEKqefl 154
Cdd:PRK10157  79 FMTEKSAMTMDYCNGDETSpsqrsYSVLRSKFDAWLMEQAE-EAGAQLITGIRVDNLVQRDGKVVGVEA-DGDVIE---- 152
                        170
                 ....*....|....
gi 446967497 155 ARLVVGADGRSSII 168
Cdd:PRK10157 153 AKTVILADGVNSIL 166
PRK07045 PRK07045
putative monooxygenase; Reviewed
2-323 1.62e-06

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 49.91  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   2 NKTYDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFPRDTLSTHTFFNNTVALLRETGVLD-------------KLLET 68
Cdd:PRK07045   3 NNPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDdvfaagglrrdamRLYHD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  69 KAPpVRDIKFQFEDTVieG---LIPevygeesCYCIRRtyldhILLEQAKSQMNVTVLEGFRVTDVIRD-DETVIGVKGL 144
Cdd:PRK07045  83 KEL-IASLDYRSASAL--GyfiLIP-------CEQLRR-----LLLAKLDGLPNVRLRFETSIERIERDaDGTVTSVTLS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 145 DGdnekqEFLA-RLVVGADGRSSIIRKLVKSELKISIPATVGIYFGYFSgfRHDNVPKFEVYKIKDNT--AILFPTNDDL 221
Cdd:PRK07045 148 DG-----ERVApTVLVGADGARSMIRDDVLRMPAERVPYATPMAFGTIA--LTDSVRECNRLYVDSNQglAYFYPIGDQA 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497 222 YVIVGIFPLEN----------KELIERLK--LNPESclrnffTDNFPNTTIGARLKNAELvepakGILGYDNYWYKGMgk 289
Cdd:PRK07045 221 TRLVVSFPADEmqgyladttrTKLLARLNefVGDES------ADAMAAIGAGTAFPLIPL-----GRMNLDRYHKRNV-- 287
                        330       340       350
                 ....*....|....*....|....*....|....
gi 446967497 290 gwALVGDAVCFKDPGMAQGIHDAICGARILSNIL 323
Cdd:PRK07045 288 --VLLGDAAHSIHPITGQGMNLAIEDAGELGACL 319
PRK08773 PRK08773
UbiH/UbiF family hydroxylase;
4-171 4.19e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181552 [Multi-domain]  Cd Length: 392  Bit Score: 45.24  E-value: 4.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   4 TYDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFPR-----DTLSTHTFFNNTVALLRETGVLDKLLETKAPPVRdiKF 78
Cdd:PRK08773   6 RRDAVIVGGGVVGAACALALADAGLSVALVEGREPPRwqadqPDLRVYAFAADNAALLDRLGVWPAVRAARAQPYR--RM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  79 QFEDTVIEGLI---PEVYGEESCYCIRRTYLdhiLLEQ---AKSQMNVTVLEGFRVTDVIRDDEtviGVKGLDGDNEKQE 152
Cdd:PRK08773  84 RVWDAGGGGELgfdADTLGREQLGWIVENDL---LVDRlwaALHAAGVQLHCPARVVALEQDAD---RVRLRLDDGRRLE 157
                        170
                 ....*....|....*....
gi 446967497 153 flARLVVGADGRSSIIRKL 171
Cdd:PRK08773 158 --AALAIAADGAASTLREL 174
PRK07364 PRK07364
FAD-dependent hydroxylase;
2-169 4.39e-05

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 45.40  E-value: 4.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   2 NKTYDVIITGARCAGSTLAIYLAKAGFHVLLV-----DRANFPRDTLSTHTFfnnTVALLRETGVLDKLL---------- 66
Cdd:PRK07364  16 SLTYDVAIVGGGIVGLTLAAALKDSGLRIALIeaqpaEAAAAKGQAYALSLL---SARIFEGIGVWEKILpqigkfrqir 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497  67 --ETKAPPVrdIKFQFEDtviegLIPEVYGeescYCIRRTYLDHILLEQAKSQMNVTVLEGFRVTDVIRDDETVigVKGL 144
Cdd:PRK07364  93 lsDADYPGV--VKFQPTD-----LGTEALG----YVGEHQVLLEALQEFLQSCPNITWLCPAEVVSVEYQQDAA--TVTL 159
                        170       180
                 ....*....|....*....|....*
gi 446967497 145 DGDNEKQEFLARLVVGADGRSSIIR 169
Cdd:PRK07364 160 EIEGKQQTLQSKLVVAADGARSPIR 184
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
5-170 6.57e-05

ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone


Pssm-ID: 273914 [Multi-domain]  Cd Length: 437  Bit Score: 44.75  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497    5 YDVIITGARCAGSTLAIYLAK----AGFHVLLVDRANFP----RDTLSTHTFFNN--------TVALLRETGVLDKLLET 68
Cdd:TIGR01989   1 FDVVIVGGGPVGLALAAALGNnpltKDLKVLLLDAVDNPklksRNYEKPDGPYSNrvssitpaSISFFKKIGAWDHIQSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446967497   69 KAPPVRdiKFQFEDTVIEGLI---PEVYGEESCYCIRRTYLDHILLEQAKSQM--NVTVLEGFRVTDV------IRDDET 137
Cdd:TIGR01989  81 RIQPFG--RMQVWDGCSLALIrfdRDNGKEDMACIIENDNIQNSLYNRLQEYNgdNVKILNPARLISVtipskyPNDNSN 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 446967497  138 VIGVKGLDGDNekqeFLARLVVGADGRSSIIRK 170
Cdd:TIGR01989 159 WVHITLSDGQV----LYTKLLIGADGSNSNVRK 187
PTZ00367 PTZ00367
squalene epoxidase; Provisional
2-38 3.98e-04

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 42.53  E-value: 3.98e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446967497   2 NKTYDVIITGARCAGSTLAIYLAKAGFHVLLVDRANF 38
Cdd:PTZ00367  31 NYDYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLF 67
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
3-35 5.91e-04

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 41.81  E-value: 5.91e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446967497   3 KTYDVIITGARCAGSTLAIYLAKAGFHVLLVDR 35
Cdd:COG0665    1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLER 33
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
3-38 9.48e-04

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 41.32  E-value: 9.48e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446967497   3 KTYDVIITGARCAGSTLAIYLAKAGFHVLLVDRANF 38
Cdd:PRK06292   2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPL 37
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
6-39 3.07e-03

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: 39.30  E-value: 3.07e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 446967497    6 DVIITGARCAGSTLAIYLAKAGFHVLLVDRANFP 39
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDP 34
solA PRK11259
N-methyl-L-tryptophan oxidase;
4-46 3.19e-03

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 39.43  E-value: 3.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446967497   4 TYDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFPRDTLSTH 46
Cdd:PRK11259   3 RYDVIVIGLGSMGSAAGYYLARRGLRVLGLDRFMPPHQQGSSH 45
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
5-46 5.03e-03

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: 38.66  E-value: 5.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446967497    5 YDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFPRDTLSTH 46
Cdd:TIGR01377   1 FDVIVVGAGIMGCFAAYHLAKHGKKTLLLEQFDLPHSRGSSH 42
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
2-39 5.80e-03

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 38.68  E-value: 5.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446967497   2 NKTYDVIITGARCAGSTLAIYLAKAGFHVLLVDRANFP 39
Cdd:COG1233    1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTP 38
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
5-35 6.53e-03

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 38.18  E-value: 6.53e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446967497   5 YDVIITGARCAGSTLAIYLAKAGFHVLLVDR 35
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG 31
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
5-37 9.62e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 38.24  E-value: 9.62e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446967497   5 YDVIITGARCAGSTLAIYLAKAGFHVLLVDRAN 37
Cdd:COG3573    6 ADVIVVGAGLAGLVAAAELADAGRRVLLLDQEP 38
 
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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