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Conserved domains on  [gi|187960045|ref|NP_003670|]
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kynurenine 3-monooxygenase isoform 1 [Homo sapiens]

Protein Classification

FAD-dependent oxidoreductase( domain architecture ID 11428987)

FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0071949|GO:0016491

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 7-364 6.61e-41

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: 149.32  E-value: 6.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   7 QRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRvatfTRGRSInlALSHRGRQALKAVGLEDQIVSQGIPMRARM 86
Cdd:COG0654    2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR----PDGRGI--ALSPRSLELLRRLGLWDRLLARGAPIRGIR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  87 IH-SLSGKK-SAIPYG-TKSQYILSVSRENLNKDLLTAAEKYpNVKMHFNHRLLKCNPEEGMITVLGSDKvpKDVTCDLI 163
Cdd:COG0654   76 VRdGSDGRVlARFDAAeTGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGVTVTLADG--RTLRADLV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 164 VGCDGAYSTVRSHLMKKPR-FDYSQQyiphgymeltippkngdyamepnylhiwprntfMMIAlpnmnksftctlfmpfe 242
Cdd:COG0654  153 VGADGARSAVRRLLGIGFTgRDYPQR---------------------------------ALWA----------------- 182

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 243 efeklltsnDVVDFFQKYFPDAIPLIGEKLLVQDFFLLpaqPMISVKCSSFHfKSHCVLLGDAAHAIVPFFGQGMNAGFE 322
Cdd:COG0654  183 ---------GVRTELRARLAAAGPRLGELLELSPRSAF---PLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALR 249

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 187960045 323 DCLVFDELMDKFSNDLSLC--LPVFSRLRIPDDHAISDLSMYNY 364
Cdd:COG0654  250 DAAALAWKLAAALRGRDDEaaLARYERERRPRAARVQRAADALG 293
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 7-364 6.61e-41

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: 149.32  E-value: 6.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   7 QRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRvatfTRGRSInlALSHRGRQALKAVGLEDQIVSQGIPMRARM 86
Cdd:COG0654    2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR----PDGRGI--ALSPRSLELLRRLGLWDRLLARGAPIRGIR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  87 IH-SLSGKK-SAIPYG-TKSQYILSVSRENLNKDLLTAAEKYpNVKMHFNHRLLKCNPEEGMITVLGSDKvpKDVTCDLI 163
Cdd:COG0654   76 VRdGSDGRVlARFDAAeTGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGVTVTLADG--RTLRADLV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 164 VGCDGAYSTVRSHLMKKPR-FDYSQQyiphgymeltippkngdyamepnylhiwprntfMMIAlpnmnksftctlfmpfe 242
Cdd:COG0654  153 VGADGARSAVRRLLGIGFTgRDYPQR---------------------------------ALWA----------------- 182

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 243 efeklltsnDVVDFFQKYFPDAIPLIGEKLLVQDFFLLpaqPMISVKCSSFHfKSHCVLLGDAAHAIVPFFGQGMNAGFE 322
Cdd:COG0654  183 ---------GVRTELRARLAAAGPRLGELLELSPRSAF---PLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALR 249

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 187960045 323 DCLVFDELMDKFSNDLSLC--LPVFSRLRIPDDHAISDLSMYNY 364
Cdd:COG0654  250 DAAALAWKLAAALRGRDDEaaLARYERERRPRAARVQRAADALG 293
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 11-323 4.89e-23

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: 100.74  E-value: 4.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   11 VAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVAT-FTRGRSInlALSHRGRQALKAVGLEDQIVsqgiPMRARMIHS 89
Cdd:TIGR01988   2 IVIVGGGMVGLALALALARSGLKVALIEATPLPAPADpGFDNRVS--ALSAASIRLLEKLGVWDKIE----PARAQPIRD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   90 L--------------SGKKSAIPYGtksqYIlsVSRENLNKDLLTAAEKYPNVKMHFNHRL--LKCNPEEGMITvLGSDK 153
Cdd:TIGR01988  76 IhvsdggsfgalrfdADEIGLEALG----YV--VENRVLQQALWERLQELPNVTLLCPARVveLPRHSDHVELT-LDDGQ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  154 VpkdVTCDLIVGCDGAYSTVRSHL-MKKPRFDYSQqyipHGY---MELTIPPKNgdYAMEpnylHIWPRNTFMMIALPNM 229
Cdd:TIGR01988 149 Q---LRARLLVGADGANSKVRQLAgIPTTGWDYGQ----SAVvanVKHERPHQG--TAWE----RFTPTGPLALLPLPDN 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  230 NKSFTCT---------LFMPFEEFEKLLTSNdvvdfFQKYFPdAIPLIGEKLLVQDFFLLPAQpmisvkcssfHFKSHCV 300
Cdd:TIGR01988 216 RSSLVWTlppeeaerlLALSDEEFLAELQRA-----FGSRLG-AITLVGERHAFPLSLTHAKR----------YVAPRLA 279

                         330       340
                  ....*....|....*....|...
gi 187960045  301 LLGDAAHAIVPFFGQGMNAGFED 323
Cdd:TIGR01988 280 LIGDAAHTIHPLAGQGLNLGLRD 302
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 10-323 1.10e-17

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: 84.30  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   10 KVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVatFTRGRSINlalsHRGRQALKAVGLEDQIVSQGIPmRARMIHS 89
Cdd:pfam01494   3 DVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSV--LPRAHGLN----QRTMELLRQAGLEDRILAEGVP-HEGMGLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   90 LSGKKSAIPYG--TKSQYILSVSRENLNKDLLTAAEKYPnVKMHFNHRLLKCNPEEGMIT---VLGSDKVPKDVTCDLIV 164
Cdd:pfam01494  76 FYNTRRRADLDflTSPPRVTVYPQTELEPILVEHAEARG-AQVRFGTEVLSLEQDGDGVTavvRDRRDGEEYTVRAKYLV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  165 GCDGAYSTVRSHLmkkpRFDY-SQQYIPHGYMELTIPPKNGDYAMEPNYLHIWPRNT----FMMIALPNMNKSFTCTLFM 239
Cdd:pfam01494 155 GCDGGRSPVRKTL----GIEFeGFEGVPFGSLDVLFDAPDLSDPVERAFVHYLIYAPhsrgFMVGPWRSAGRERYYVQVP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  240 PFEEFEKllTSNDVvdFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKShcVLL-GDAAHAIVPFFGQGMN 318
Cdd:pfam01494 231 WDEEVEE--RPEEF--TDEELKQRLRSIVGIDLALVEILWKSIWGVASRVATRYRKGR--VFLaGDAAHIHPPTGGQGLN 304


                  ....*
gi 187960045  319 AGFED 323
Cdd:pfam01494 305 TAIQD 309
PRK07364 PRK07364
FAD-dependent hydroxylase;
11-323 4.79e-14

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 73.90  E-value: 4.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  11 VAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATftRGRSinLALSHRGRQALKAVGLEDQIVSQGIPMRaRMIHSL 90
Cdd:PRK07364  21 VAIVGGGIVGLTLAAALKDSGLRIALIEAQPAEAAAA--KGQA--YALSLLSARIFEGIGVWEKILPQIGKFR-QIRLSD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  91 SGKKSAIPYGT---KSQYILSVSREN-LNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITV-LGSDKVPKDVTCDLIVG 165
Cdd:PRK07364  96 ADYPGVVKFQPtdlGTEALGYVGEHQvLLEALQEFLQSCPNITWLCPAEVVSVEYQQDAATVtLEIEGKQQTLQSKLVVA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 166 CDGAYSTVRSHLMKKPR-FDYSQQYIphgymELTIPPK--NGDYAMEpnylHIWPRNTFMMIALPNMNKSFTCTlfMPFE 242
Cdd:PRK07364 176 ADGARSPIRQAAGIKTKgWKYWQSCV-----TATVKHEapHNDIAYE----RFWPSGPFAILPLPGNRCQIVWT--APHA 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 243 EFEKL--LTSNDVVDFFQKYFPDaipLIGEKLLVQDFFLLPAQPMISVKcssfHFKSHCVLLGDAAHAIVPFFGQGMNAG 320
Cdd:PRK07364 245 QAKALlaLPEAEFLAELQQRYGD---QLGKLELLGDRFLFPVQLMQSDR----YVQHRLALVGDAAHCCHPVGGQGLNLG 317


                 ...
gi 187960045 321 FED 323
Cdd:PRK07364 318 IRD 320
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 7-364 6.61e-41

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: 149.32  E-value: 6.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   7 QRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRvatfTRGRSInlALSHRGRQALKAVGLEDQIVSQGIPMRARM 86
Cdd:COG0654    2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR----PDGRGI--ALSPRSLELLRRLGLWDRLLARGAPIRGIR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  87 IH-SLSGKK-SAIPYG-TKSQYILSVSRENLNKDLLTAAEKYpNVKMHFNHRLLKCNPEEGMITVLGSDKvpKDVTCDLI 163
Cdd:COG0654   76 VRdGSDGRVlARFDAAeTGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGVTVTLADG--RTLRADLV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 164 VGCDGAYSTVRSHLMKKPR-FDYSQQyiphgymeltippkngdyamepnylhiwprntfMMIAlpnmnksftctlfmpfe 242
Cdd:COG0654  153 VGADGARSAVRRLLGIGFTgRDYPQR---------------------------------ALWA----------------- 182

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 243 efeklltsnDVVDFFQKYFPDAIPLIGEKLLVQDFFLLpaqPMISVKCSSFHfKSHCVLLGDAAHAIVPFFGQGMNAGFE 322
Cdd:COG0654  183 ---------GVRTELRARLAAAGPRLGELLELSPRSAF---PLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALR 249

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 187960045 323 DCLVFDELMDKFSNDLSLC--LPVFSRLRIPDDHAISDLSMYNY 364
Cdd:COG0654  250 DAAALAWKLAAALRGRDDEaaLARYERERRPRAARVQRAADALG 293
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 11-323 4.89e-23

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: 100.74  E-value: 4.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   11 VAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVAT-FTRGRSInlALSHRGRQALKAVGLEDQIVsqgiPMRARMIHS 89
Cdd:TIGR01988   2 IVIVGGGMVGLALALALARSGLKVALIEATPLPAPADpGFDNRVS--ALSAASIRLLEKLGVWDKIE----PARAQPIRD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   90 L--------------SGKKSAIPYGtksqYIlsVSRENLNKDLLTAAEKYPNVKMHFNHRL--LKCNPEEGMITvLGSDK 153
Cdd:TIGR01988  76 IhvsdggsfgalrfdADEIGLEALG----YV--VENRVLQQALWERLQELPNVTLLCPARVveLPRHSDHVELT-LDDGQ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  154 VpkdVTCDLIVGCDGAYSTVRSHL-MKKPRFDYSQqyipHGY---MELTIPPKNgdYAMEpnylHIWPRNTFMMIALPNM 229
Cdd:TIGR01988 149 Q---LRARLLVGADGANSKVRQLAgIPTTGWDYGQ----SAVvanVKHERPHQG--TAWE----RFTPTGPLALLPLPDN 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  230 NKSFTCT---------LFMPFEEFEKLLTSNdvvdfFQKYFPdAIPLIGEKLLVQDFFLLPAQpmisvkcssfHFKSHCV 300
Cdd:TIGR01988 216 RSSLVWTlppeeaerlLALSDEEFLAELQRA-----FGSRLG-AITLVGERHAFPLSLTHAKR----------YVAPRLA 279

                         330       340
                  ....*....|....*....|...
gi 187960045  301 LLGDAAHAIVPFFGQGMNAGFED 323
Cdd:TIGR01988 280 LIGDAAHTIHPLAGQGLNLGLRD 302
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 10-323 1.10e-17

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: 84.30  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   10 KVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVatFTRGRSINlalsHRGRQALKAVGLEDQIVSQGIPmRARMIHS 89
Cdd:pfam01494   3 DVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSV--LPRAHGLN----QRTMELLRQAGLEDRILAEGVP-HEGMGLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   90 LSGKKSAIPYG--TKSQYILSVSRENLNKDLLTAAEKYPnVKMHFNHRLLKCNPEEGMIT---VLGSDKVPKDVTCDLIV 164
Cdd:pfam01494  76 FYNTRRRADLDflTSPPRVTVYPQTELEPILVEHAEARG-AQVRFGTEVLSLEQDGDGVTavvRDRRDGEEYTVRAKYLV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  165 GCDGAYSTVRSHLmkkpRFDY-SQQYIPHGYMELTIPPKNGDYAMEPNYLHIWPRNT----FMMIALPNMNKSFTCTLFM 239
Cdd:pfam01494 155 GCDGGRSPVRKTL----GIEFeGFEGVPFGSLDVLFDAPDLSDPVERAFVHYLIYAPhsrgFMVGPWRSAGRERYYVQVP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  240 PFEEFEKllTSNDVvdFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKShcVLL-GDAAHAIVPFFGQGMN 318
Cdd:pfam01494 231 WDEEVEE--RPEEF--TDEELKQRLRSIVGIDLALVEILWKSIWGVASRVATRYRKGR--VFLaGDAAHIHPPTGGQGLN 304


                  ....*
gi 187960045  319 AGFED 323
Cdd:pfam01494 305 TAIQD 309
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
16-216 7.09e-17

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 80.78  E-value: 7.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  16 GGLVGSLQACFLAKRNFQIDVYEAREdtrvatFTRGRSINLALSHRGRQALKAVGLEDQIVSqgiPMRARMIHSLSGKKS 95
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGS------FPGDKICGGGLLPRALEELEPLGLDEPLER---PVRGARFYSPGGKSV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  96 AIPYGTKSQYIlsVSRENLNKDLLTAAEKYpNVKMHFNHRLLKCNPEEGMITVLGSDkvPKDVTCDLIVGCDGAYSTVRS 175
Cdd:COG0644   72 ELPPGRGGGYV--VDRARFDRWLAEQAEEA-GAEVRTGTRVTDVLRDDGRVVVRTGD--GEEIRADYVVDADGARSLLAR 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 187960045 176 HLMKKPRFDYSQQYIpHGYMELTIPPKNGDYamEPNYLHIW 216
Cdd:COG0644  147 KLGLKRRSDEPQDYA-LAIKEHWELPPLEGV--DPGAVEFF 184
PRK07364 PRK07364
FAD-dependent hydroxylase;
11-323 4.79e-14

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 73.90  E-value: 4.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  11 VAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATftRGRSinLALSHRGRQALKAVGLEDQIVSQGIPMRaRMIHSL 90
Cdd:PRK07364  21 VAIVGGGIVGLTLAAALKDSGLRIALIEAQPAEAAAA--KGQA--YALSLLSARIFEGIGVWEKILPQIGKFR-QIRLSD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  91 SGKKSAIPYGT---KSQYILSVSREN-LNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITV-LGSDKVPKDVTCDLIVG 165
Cdd:PRK07364  96 ADYPGVVKFQPtdlGTEALGYVGEHQvLLEALQEFLQSCPNITWLCPAEVVSVEYQQDAATVtLEIEGKQQTLQSKLVVA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 166 CDGAYSTVRSHLMKKPR-FDYSQQYIphgymELTIPPK--NGDYAMEpnylHIWPRNTFMMIALPNMNKSFTCTlfMPFE 242
Cdd:PRK07364 176 ADGARSPIRQAAGIKTKgWKYWQSCV-----TATVKHEapHNDIAYE----RFWPSGPFAILPLPGNRCQIVWT--APHA 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 243 EFEKL--LTSNDVVDFFQKYFPDaipLIGEKLLVQDFFLLPAQPMISVKcssfHFKSHCVLLGDAAHAIVPFFGQGMNAG 320
Cdd:PRK07364 245 QAKALlaLPEAEFLAELQQRYGD---QLGKLELLGDRFLFPVQLMQSDR----YVQHRLALVGDAAHCCHPVGGQGLNLG 317


                 ...
gi 187960045 321 FED 323
Cdd:PRK07364 318 IRD 320
PRK07045 PRK07045
putative monooxygenase; Reviewed
 11-356 4.97e-12

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 67.24  E-value: 4.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  11 VAVIGGGLVGSLQACFLAKRNFQIDVYEaredtRVAtftRGRSINLA--LSHRGRQALKAVGLEDQIVSQGIPMRARM-I 87
Cdd:PRK07045   8 VLINGSGIAGVALAHLLGARGHSVTVVE-----RAA---RNRAQNGAdlLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  88 HSLSGKKSAIPYGTKSQ--YILSVSRENLNKDLLTAAEKYPNVKMHFNHRLLKCNPEE-GMITVL----GSDKVPKdvtc 160
Cdd:PRK07045  80 YHDKELIASLDYRSASAlgYFILIPCEQLRRLLLAKLDGLPNVRLRFETSIERIERDAdGTVTSVtlsdGERVAPT---- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 161 dLIVGCDGAYSTVRSHLMKKP--RFDYSQQyIPHGYMELTippkngDYAMEPNYLHIwPRNTFMMIALPNMNKSFTCTLF 238
Cdd:PRK07045 156 -VLVGADGARSMIRDDVLRMPaeRVPYATP-MAFGTIALT------DSVRECNRLYV-DSNQGLAYFYPIGDQATRLVVS 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 239 MPFEEFEKLL---TSNDVVDFFQKYF----PDAIPLIGEKllvQDFFLLPAQPMisvKCSSFHfKSHCVLLGDAAHAIVP 311
Cdd:PRK07045 227 FPADEMQGYLadtTRTKLLARLNEFVgdesADAMAAIGAG---TAFPLIPLGRM---NLDRYH-KRNVVLLGDAAHSIHP 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 187960045 312 FFGQGMNAGFEDCLVFDELMDKFSND---LSLCLPVFSRLRIPDDHAI 356
Cdd:PRK07045 300 ITGQGMNLAIEDAGELGACLDLHLSGqiaLADALERFERIRRPVNEAV 347
PRK06753 PRK06753
hypothetical protein; Provisional
 10-351 2.88e-11

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 65.10  E-value: 2.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  10 KVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVAtftrGRSINLAlsHRGRQALKAVGLEDQIVSQGIPMRARMIHS 89
Cdd:PRK06753   2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESVKEV----GAGIGIG--DNVIKKLGNHDLAKGIKNAGQILSTMNLLD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  90 LSGK---KSAIPYGTKSqyiLSVSRENLNKDLLTaaeKYPNVKMHFNHRLLKCNPEEGMITVLGSDKVPKDVtcDLIVGC 166
Cdd:PRK06753  76 DKGTllnKVKLKSNTLN---VTLHRQTLIDIIKS---YVKEDAIFTGKEVTKIENETDKVTIHFADGESEAF--DLCIGA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 167 DGAYSTVRSHLMKKPRFDYsQQYIPHGYMELTIPPKNGDYAMEpnylhIW-PRNTFMMIALPNmNKSFTCTLFMPFEEFE 245
Cdd:PRK06753 148 DGIHSKVRQSVNADSKVRY-QGYTCFRGLIDDIDLKLPDCAKE-----YWgTKGRFGIVPLLN-NQAYWFITINAKERDP 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 246 KL--LTSNDVVDFFqKYFPDAIPLI-----GEKLLVQDFFLLpaQPMisvkcSSFhFKSHCVLLGDAAHAIVPFFGQGMN 318
Cdd:PRK06753 221 KYssFGKPHLQAYF-NHYPNEVREIldkqsETGILHHDIYDL--KPL-----KSF-VYGRIVLLGDAAHATTPNMGQGAG 291

                        330       340       350
                 ....*....|....*....|....*....|...
gi 187960045 319 AGFEDCLVFDELMDKFsnDLSLCLPVFSRLRIP 351
Cdd:PRK06753 292 QAMEDAIVLANCLNAY--DFEKALQRYDKIRVK 322
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 11-323 7.25e-11

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: 64.01  E-value: 7.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   11 VAVIGGGLVGSLQACFLA-------KRNFQIDVYEAREDTRVATFTRGRSIN---LALSHRGRQALKAVGLEDQIVSQGI 80
Cdd:TIGR01989   3 VVIVGGGPVGLALAAALGnnpltkdLKVLLLDAVDNPKLKSRNYEKPDGPYSnrvSSITPASISFFKKIGAWDHIQSDRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   81 PMRARMIHSLSGKKSAIPY--GTKSQYILSVSrENLN--KDLLTAAEKYP--NVKMHFNHRLLKC-------NPEEGMIT 147
Cdd:TIGR01989  83 QPFGRMQVWDGCSLALIRFdrDNGKEDMACII-ENDNiqNSLYNRLQEYNgdNVKILNPARLISVtipskypNDNSNWVH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  148 VLGSDKvpKDVTCDLIVGCDGAYSTVRSHL-MKKPRFDYSQQYIPhGYMELTIPPKNgdyamEPNYLHIWPRNTFMMIAL 226
Cdd:TIGR01989 162 ITLSDG--QVLYTKLLIGADGSNSNVRKAAnIDTTGWNYNQHAVV-ATLKLEEATEN-----DVAWQRFLPTGPIALLPL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  227 PNMNKSFTCT---------LFMPFEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQ------P--MISVK 289
Cdd:TIGR01989 234 PDNNSTLVWStspeealrlLSLPPEDFVDALNAAFDLGYSDHPYSYLLDYAMEKLNEDIGFRTEGSkscfqvPprVIGVV 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 187960045  290 CSS---F---------HFKSHCVLLGDAAHAIVPFFGQGMNAGFED 323
Cdd:TIGR01989 314 DKSraaFplglghadeYVTKRVALVGDAAHRVHPLAGQGVNLGFGD 359
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
11-323 1.55e-10

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 63.00  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  11 VAVIGGGLVGSLQACFLAKRNFQIDVYEaREDTrvaTFTRGRSInlALSHRGRQALKAVGLEDQIVSQGIP---MR---A 84
Cdd:PRK06183  13 VVIVGAGPVGLTLANLLGQYGVRVLVLE-RWPT---LYDLPRAV--GIDDEALRVLQAIGLADEVLPHTTPnhgMRfldA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  85 RMIHSLSGKKSAI-PYGtksqyilsVSREN------LNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITVL--GSDKVP 155
Cdd:PRK06183  87 KGRCLAEIARPSTgEFG--------WPRRNafhqplLEAVLRAGLARFPHVRVRFGHEVTALTQDDDGVTVTltDADGQR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 156 KDVTCDLIVGCDGAYSTVRSHlMKKPRFDYSQqyiPHGYMELTIPPKNGDYAMEPNYLHIWPRNTFMMIALPNMNKSFTC 235
Cdd:PRK06183 159 ETVRARYVVGCDGANSFVRRT-LGVPFEDLTF---PERWLVVDVLIANDPLGGPHTYQYCDPARPYTSVRLPHGRRRWEF 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 236 TLfMPFEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQpmisvkcssfHFKSHCVLL-GDAAHAIVPFFG 314
Cdd:PRK06183 235 ML-LPGETEEQLASPENVWRLLAPWGPTPDDAELIRHAVYTFHARVAD----------RWRSGRVLLaGDAAHLMPPFAG 303


                 ....*....
gi 187960045 315 QGMNAGFED 323
Cdd:PRK06183 304 QGMNSGIRD 312
PRK06126 PRK06126
hypothetical protein; Provisional
 8-323 3.05e-10

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 62.32  E-value: 3.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   8 RKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRV---ATFTRGRSinlaLSHRGRqalkaVGLEDQIVSQGIPM-- 82
Cdd:PRK06126   7 ETPVLIVGGGPVGLALALDLGRRGVDSILVERKDGTAFnpkANTTSARS----MEHFRR-----LGIADEVRSAGLPVdy 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  83 -------------------------RARMIHSLSGKKSAipygtkSQYILSVSRENLNKDLLTAAEKYPNVKMHFNHRLL 137
Cdd:PRK06126  78 ptdiayftrltgyelarfrlpsareAITPVGGPDGSWPS------PELPHRIPQKYLEPILLEHAAAQPGVTLRYGHRLT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 138 KCNPEEGMITV----LGSDKvPKDVTCDLIVGCDGAYSTVRSHL-----------------MKKPRFdysQQYIPH--GY 194
Cdd:PRK06126 152 DFEQDADGVTAtvedLDGGE-SLTIRADYLVGCDGARSAVRRSLgisyegtsglqrdlsiyIRAPGL---AALVGHdpAW 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 195 MELTIppkNGDYAMepNYLHIWPRNTFMMIALpnmnksftctlfmPFEEFEKLLTSNDVVDFFQKyfpdaipLIGEKLlv 274
Cdd:PRK06126 228 MYWLF---NPDRRG--VLVAIDGRDEWLFHQL-------------RGGEDEFTIDDVDARAFVRR-------GVGEDI-- 280

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 187960045 275 qDFFLLPAQPMISVKCSSFHF-KSHCVLLGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK06126 281 -DYEVLSVVPWTGRRLVADSYrRGRVFLAGDAAHLFTPTGGYGMNTGIGD 329
PRK07538 PRK07538
hypothetical protein; Provisional
 10-177 1.24e-09

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 59.91  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  10 KVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRvatfTRGRSINLaLSHRGRQaLKAVGLEDQIVSQGIPMRARMIHS 89
Cdd:PRK07538   2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEAAPELR----PLGVGINL-LPHAVRE-LAELGLLDALDAIGIRTRELAYFN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  90 LSGKKsaI---PYGTKSQYI---LSVSRENLNKDLLTAA-EKYPNVKMHFNHRLLKCNPEEGMITVL---GSDKVPKDVT 159
Cdd:PRK07538  76 RHGQR--IwsePRGLAAGYDwpqYSIHRGELQMLLLDAVrERLGPDAVRTGHRVVGFEQDADVTVVFlgdRAGGDLVSVR 153

                        170
                 ....*....|....*...
gi 187960045 160 CDLIVGCDGAYSTVRSHL 177
Cdd:PRK07538 154 GDVLIGADGIHSAVRAQL 171
PRK06847 PRK06847
hypothetical protein; Provisional
 9-330 7.74e-09

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 57.58  E-value: 7.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   9 KKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVatftRGRSINL---ALshrgrQALKAVGLEDQIVSQGIPMRAR 85
Cdd:PRK06847   5 KKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRV----YGAGITLqgnAL-----RALRELGVLDECLEAGFGFDGV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  86 MIHSLSGKKSA-----------IPYGtksqyiLSVSRENLNKDLLTAAEKyPNVKMHFNHRLLKCNPEEGMITVLGSDKv 154
Cdd:PRK06847  76 DLFDPDGTLLAelptprlagddLPGG------GGIMRPALARILADAARA-AGADVRLGTTVTAIEQDDDGVTVTFSDG- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 155 pKDVTCDLIVGCDGAYSTVRSHLM---KKPRF----------------DYSQQYIP-------------HGYMELTIPPK 202
Cdd:PRK06847 148 -TTGRYDLVVGADGLYSKVRSLVFpdePEPEYtgqgvwravlprpaevDRSLMYLGpttkagvvplsedLMYLFVTEPRP 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 203 nGDYAMEPnylHIWPRntfmmiALPNMNKSFTCTLfmpFEEFEKLLTSNDVVDFfqkyfpdaIPLigEKLLVQdffllpa 282
Cdd:PRK06847 227 -DNPRIEP---DTLAA------LLRELLAPFGGPV---LQELREQITDDAQVVY--------RPL--ETLLVP------- 276

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 187960045 283 QPMisvkcssfhFKSHCVLLGDAAHAIVPFFGQGMNAGFEDCLVF-DEL 330
Cdd:PRK06847 277 APW---------HRGRVVLIGDAAHATTPHLAQGAGMAIEDAIVLaEEL 316
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 294-353 3.11e-07

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 52.47  E-value: 3.11e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 294 HFKSHCVLLGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFSNDLSLCLPVFSRLRIPDD 353
Cdd:PRK08849 276 YVKNNCVLLGDAAHTINPLAGQGVNLGFKDVDVLLAETEKQGVLNDASFARYERRRRPDN 335
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 11-190 4.41e-07

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 52.55  E-value: 4.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  11 VAVIGGGLVGSLQACFLAKRNFQIDVYEaredtRVATFTRGRSINLALSHRGRQALKAVGLEDQIVSQGIPMRARMIHSL 90
Cdd:PTZ00367  36 VIIVGGSIAGPVLAKALSKQGRKVLMLE-----RDLFSKPDRIVGELLQPGGVNALKELGMEECAEGIGMPCFGYVVFDH 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  91 SGKKSAIPYGTKSQ---------------YILSVSREN-----------LNKDL----------LTAAEKYPNVKMHFNH 134
Cdd:PTZ00367 111 KGKQVKLPYGAGASgvsfhfgdfvqnlrsHVFHNCQDNvtmlegtvnslLEEGPgfseraygveYTEAEKYDVPENPFRE 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 187960045 135 RLLKCNPEEGMITvlgsdkvpKDVTCDLIVGCDGAYSTVRSHLMK-KPRFDYSQQYI 190
Cdd:PTZ00367 191 DPPSANPSATTVR--------KVATAPLVVMCDGGMSKFKSRYQHyTPASENHSHFV 239
PRK06475 PRK06475
FAD-binding protein;
13-351 1.28e-05

FAD-binding protein;


Pssm-ID: 180582 [Multi-domain]  Cd Length: 400  Bit Score: 47.51  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  13 VIGGGLVGSLQACFLAKRNFQIDVYEAREDTRvatfTRGRSINL---ALSHRGR----QALKAVGLEDQIVS--QGIPMR 83
Cdd:PRK06475   7 IAGAGVAGLSAALELAARGWAVTIIEKAQELS----EVGAGLQLapnAMRHLERlgvaDRLSGTGVTPKALYlmDGRKAR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  84 ARM---IHSLSGKKSAIPYgtksqyiLSVSRENLNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITV-LGSDKVPKDVT 159
Cdd:PRK06475  83 PLLamqLGDLARKRWHHPY-------IVCHRADLQSALLDACRNNPGIEIKLGAEMTSQRQTGNSITAtIIRTNSVETVS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 160 CDLIVGCDGAYSTVRShlmKKP--RFDYSQQYIPHGYMELTIPPKNGDYAM-EPNYLHIW--PRNTFmmIALP-NMNKSF 233
Cdd:PRK06475 156 AAYLIACDGVWSMLRA---KAGfsKARFSGHIAWRTTLAADALPASFLSAMpEHKAVSAWlgNKAHF--IAYPvKGGKFF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 234 TCTLFMPFEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFllPAQPMISVKCSSFHFKSHCVLLGDAAHAIVPFF 313
Cdd:PRK06475 231 NFVAITGGENPGEVWSKTGDKAHLKSIYADWNKPVLQILAAIDEW--TYWPLFEMADAQFVGPDRTIFLGDASHAVTPFA 308

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 187960045 314 GQGMNAGFEDCLVFDELMDkfSNDLSLCLPVFSRLRIP 351
Cdd:PRK06475 309 AQGAAMAIEDAAALAEALD--SDDQSAGLKRFDSVRKE 344
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
13-51 1.59e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 42.52  E-value: 1.59e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 187960045   13 VIGGGLVGSLQACFLAKRNFQIDVYEAREDT--RVATFTRG 51
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLggNAYSYRVP 41
PRK05732 PRK05732
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
 11-187 2.01e-05

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 235584 [Multi-domain]  Cd Length: 395  Bit Score: 46.77  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  11 VAVIGGGLVGS-----LQAcfLAKRNFQIDVYEARE--DTRVATFTrGRSInlALSHRGRQALKAVGLEDQIVSQGIPMR 83
Cdd:PRK05732   6 VIIVGGGMAGAtlalaLSR--LSHGGLPVALIEAFApeSDAHPGFD-ARAI--ALAAGTCQQLARLGVWQALADCATPIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  84 ArmIH-SLSGKKS-----AIPYGTKS-QYIlsVSRENLNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITV-LGSDKVp 155
Cdd:PRK05732  81 H--IHvSDRGHAGfvrldAEDYGVPAlGYV--VELHDVGQRLFALLDKAPGVTLHCPARVANVERTQGSVRVtLDDGET- 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 187960045 156 kdVTCDLIVGCDGAYSTVRSHL-MKKPRFDYSQ 187
Cdd:PRK05732 156 --LTGRLLVAADGSHSALREALgIDWQQHPYEQ 186
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
7-182 3.75e-05

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 45.80  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   7 QRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEaredtRVATFTR-GRSINLALShrGRQALKAVGLEDQIVSQGI-PMRA 84
Cdd:PRK08163   3 KVTPVLIVGGGIGGLAAALALARQGIKVKLLE-----QAAEIGEiGAGIQLGPN--AFSALDALGVGEAARQRAVfTDHL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  85 RMIHSLSGKKSA-IPYGTKSQ------YILsVSRENLNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITVLgsDKVPKD 157
Cdd:PRK08163  76 TMMDAVDAEEVVrIPTGQAFRarfgnpYAV-IHRADIHLSLLEAVLDHPLVEFRTSTHVVGIEQDGDGVTVF--DQQGNR 152

                        170       180
                 ....*....|....*....|....*.
gi 187960045 158 VTCDLIVGCDGAYSTVRSHLM-KKPR 182
Cdd:PRK08163 153 WTGDALIGCDGVKSVVRQSLVgDAPR 178
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
296-323 7.68e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 44.94  E-value: 7.68e-05
                         10        20
                 ....*....|....*....|....*...
gi 187960045 296 KSHCVLLGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK07608 279 APRVALVGDAAHLIHPLAGQGMNLGLRD 306
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
7-72 1.21e-04

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 44.13  E-value: 1.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187960045   7 QRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATFTRGRSINLALSHRGRQALKAVGLE 72
Cdd:COG0665    1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGASGRNAGQLRPGLAALADRALVRLARE 66
PRK06185 PRK06185
FAD-dependent oxidoreductase;
11-318 2.89e-04

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 43.31  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  11 VAVIGGGLVGSLQACFLAKRNFQIDVYEAREDtrvatFTRgrsinlalSHRG-------RQALKAVGLEDQIVsqGIP-M 82
Cdd:PRK06185   9 CCIVGGGPAGMMLGLLLARAGVDVTVLEKHAD-----FLR--------DFRGdtvhpstLELMDELGLLERFL--ELPhQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045  83 RARMIHSLSGKK-------SAIPygTKSQYILSVSRenlnKDLL----TAAEKYPNVKMHFNHR---LLKcnpEEGMIT- 147
Cdd:PRK06185  74 KVRTLRFEIGGRtvtladfSRLP--TPYPYIAMMPQ----WDFLdflaEEASAYPNFTLRMGAEvtgLIE---EGGRVTg 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 148 -VLGSDKVPKDVTCDLIVGCDGAYSTVRshlmKKPRFDYSQQYIPHGYMELTIPPKNGDyamePNYL--HIWPRNtfMMI 224
Cdd:PRK06185 145 vRARTPDGPGEIRADLVVGADGRHSRVR----ALAGLEVREFGAPMDVLWFRLPREPDD----PESLmgRFGPGQ--GLI 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045 225 ALPNMNKsFTCTLFMPFEEFEKLltSNDVVDFFQKYFPDAIPLIGEKLLV----QDFFLLpaqpmiSVKCSsfHFKS-HC 299
Cdd:PRK06185 215 MIDRGDY-WQCGYVIPKGGYAAL--RAAGLEAFRERVAELAPELADRVAElkswDDVKLL------DVRVD--RLRRwHR 283

                        330       340
                 ....*....|....*....|..
gi 187960045 300 ---VLLGDAAHAIVPFFGQGMN 318
Cdd:PRK06185 284 pglLCIGDAAHAMSPVGGVGIN 305
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 3-47 4.01e-04

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: 42.91  E-value: 4.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 187960045   3 SSVIQRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAreDTRVAT 47
Cdd:PRK01747 255 PGSPKARDAAIIGGGIAGAALALALARRGWQVTLYEA--DEAPAQ 297
PRK08013 PRK08013
oxidoreductase; Provisional
 295-323 6.80e-04

oxidoreductase; Provisional


Pssm-ID: 236139 [Multi-domain]  Cd Length: 400  Bit Score: 41.95  E-value: 6.80e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 187960045 295 FKSH-CVLLGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK08013 279 FAAHrLALVGDAAHTIHPLAGQGVNLGFMD 308
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 8-40 7.82e-04

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 41.76  E-value: 7.82e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 187960045   8 RKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAR 40
Cdd:COG3349    3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEAR 35
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 300-332 8.34e-04

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 41.51  E-value: 8.34e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 187960045 300 VLLGDAAHAIVPFFGQGMNAGFEDClvfDELMD 332
Cdd:PRK08020 284 ALVGDAAHTINPLAGQGVNLGYRDV---DALLD 313
PRK05714 PRK05714
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 279-331 9.11e-04

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 168201 [Multi-domain]  Cd Length: 405  Bit Score: 41.74  E-value: 9.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 187960045 279 LLPAQPMISVKCSSFHFKSHC----VLLGDAAHAIVPFFGQGMNAGFEDCLVFDELM 331
Cdd:PRK05714 263 VLSADPRLCVPLRQRHAKRYVepglALIGDAAHTIHPLAGQGVNLGFLDAAVLAEVL 319
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 10-42 2.16e-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: 40.07  E-value: 2.16e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 187960045   10 KVAVIGGGLVGSLQACFLAKRNFQIDVYEARED 42
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDD 33
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
301-323 2.67e-03

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 39.96  E-value: 2.67e-03
                         10        20
                 ....*....|....*....|...
gi 187960045 301 LLGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK07333 284 LVGDAAHGIHPIAGQGLNLGLKD 306
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 8-76 5.10e-03

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: 39.05  E-value: 5.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960045   8 RKKVAVIGGGLVGsLQACF-LAKRNFQIDVYEAreDTRV----ATFTR-GRSI----NLALSHRG--RQALKAVGLEDQI 75
Cdd:COG1232    1 MKRVAVIGGGIAG-LTAAYrLAKAGHEVTVLEA--SDRVggliRTVEVdGFRIdrgpHSFLTRDPevLELLRELGLGDEL 77


                 .
gi 187960045  76 V 76
Cdd:COG1232   78 V 78
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 7-75 5.70e-03

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 39.06  E-value: 5.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187960045   7 QRKKVAVIGGGLvGSLQ-ACFLAKRNFQIDVYEAREDT--RVATFTR-GRSINLALS-----HRGRQALKAVGLEDQI 75
Cdd:COG1233    2 MMYDVVVIGAGI-GGLAaAALLARAGYRVTVLEKNDTPggRARTFERpGFRFDVGPSvltmpGVLERLFRELGLEDYL 78
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 9-40 6.73e-03

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 38.97  E-value: 6.73e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 187960045   9 KKVAVIGGGLVGSLQACFLAKRNFQIDVYEAR 40
Cdd:PRK05335   3 KPVNVIGAGLAGSEAAWQLAKRGVPVELYEMR 34
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 8-40 8.00e-03

Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440819  Cd Length: 436  Bit Score: 38.50  E-value: 8.00e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 187960045   8 RKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAR 40
Cdd:COG1206    1 MKPVTVIGGGLAGSEAAWQLAERGVPVRLYEMR 33
PRK13984 PRK13984
putative oxidoreductase; Provisional
 9-40 9.64e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 38.59  E-value: 9.64e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 187960045   9 KKVAVIGGGLVGSLQACFLAKRNFQIDVYEAR 40
Cdd:PRK13984 284 KKVAIVGSGPAGLSAAYFLATMGYEVTVYESL 315
 
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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