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Conserved domains on  [gi|1958673202|ref|XP_038946975|]
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kynurenine 3-monooxygenase isoform X6 [Rattus norvegicus]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11428987)

NAD(P)/FAD-dependent oxidoreductase catalyzes the hydroxylation of specific substrates; similar to kynurenine 3-monooxygenase which catalyzes the hydroxylation of L-kynurenine to form 3-hydroxy-L-kynurenine

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 ...
 45-157 6.22e-10

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: 59.18  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673202  45 DVLDFFQKNFPDAIPLMGEqalMRDFFLLPAQPMISVKCSPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELM 124
Cdd:COG0654   183 GVRTELRARLAAAGPRLGE---LLELSPRSAFPLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKL 258

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958673202 125 DKF--NNDLSVCLPEFSRFRIPDDHAISDLSMYNY 157
Cdd:COG0654   259 AAAlrGRDDEAALARYERERRPRAARVQRAADALG 293
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 45-157 6.22e-10

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: 59.18  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673202  45 DVLDFFQKNFPDAIPLMGEqalMRDFFLLPAQPMISVKCSPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELM 124
Cdd:COG0654   183 GVRTELRARLAAAGPRLGE---LLELSPRSAFPLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKL 258

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958673202 125 DKF--NNDLSVCLPEFSRFRIPDDHAISDLSMYNY 157
Cdd:COG0654   259 AAAlrGRDDEAALARYERERRPRAARVQRAADALG 293
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 89-146 1.41e-07

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


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 52.08  E-value: 1.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958673202  89 KSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKfNNDLSVCLPE-FSRFRIPDD 146
Cdd:PRK08849  278 KNNCVLLGDAAHTINPLAGQGVNLGFKDVDVLLAETEK-QGVLNDASFArYERRRRPDN 335
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 87-116 3.00e-04

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: 42.05  E-value: 3.00e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958673202  87 HLKSRCVLMGDAAHAIVPFFGQGMNAGFED 116
Cdd:TIGR01989 330 YVTKRVALVGDAAHRVHPLAGQGVNLGFGD 359
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 45-157 6.22e-10

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: 59.18  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673202  45 DVLDFFQKNFPDAIPLMGEqalMRDFFLLPAQPMISVKCSPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELM 124
Cdd:COG0654   183 GVRTELRARLAAAGPRLGE---LLELSPRSAFPLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKL 258

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958673202 125 DKF--NNDLSVCLPEFSRFRIPDDHAISDLSMYNY 157
Cdd:COG0654   259 AAAlrGRDDEAALARYERERRPRAARVQRAADALG 293
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 89-146 1.41e-07

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


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 52.08  E-value: 1.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958673202  89 KSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKfNNDLSVCLPE-FSRFRIPDD 146
Cdd:PRK08849  278 KNNCVLLGDAAHTINPLAGQGVNLGFKDVDVLLAETEK-QGVLNDASFArYERRRRPDN 335
PRK07364 PRK07364
FAD-dependent hydroxylase;
44-116 1.18e-06

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 49.25  E-value: 1.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958673202  44 SDVLDFFQKNFPDaipLMGEQALMRDFFLLPAQPMISVKcspfHLKSRCVLMGDAAHAIVPFFGQGMNAGFED 116
Cdd:PRK07364  255 AEFLAELQQRYGD---QLGKLELLGDRFLFPVQLMQSDR----YVQHRLALVGDAAHCCHPVGGQGLNLGIRD 320
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
89-116 3.05e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 44.94  E-value: 3.05e-05
                          10        20
                  ....*....|....*....|....*...
gi 1958673202  89 KSRCVLMGDAAHAIVPFFGQGMNAGFED 116
Cdd:PRK07608  279 APRVALVGDAAHLIHPLAGQGMNLGLRD 306
PRK07045 PRK07045
putative monooxygenase; Reviewed
 89-149 3.25e-05

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 44.90  E-value: 3.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958673202  89 KSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFNND---LSVCLPEFSRFRIPDDHAI 149
Cdd:PRK07045  284 KRNVVLLGDAAHSIHPITGQGMNLAIEDAGELGACLDLHLSGqiaLADALERFERIRRPVNEAV 347
PRK06753 PRK06753
hypothetical protein; Provisional
 52-144 3.69e-05

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 44.68  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673202  52 KNFPDAIPLMGEQA-----LMRDFFLLpaQPMISvkcspfHLKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVfdeLMDK 126
Cdd:PRK06753  235 NHYPNEVREILDKQsetgiLHHDIYDL--KPLKS------FVYGRIVLLGDAAHATTPNMGQGAGQAMEDAIV---LANC 303

                          90
                  ....*....|....*....
gi 1958673202 127 FNN-DLSVCLPEFSRFRIP 144
Cdd:PRK06753  304 LNAyDFEKALQRYDKIRVK 322
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
91-116 3.85e-05

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 44.90  E-value: 3.85e-05
                          10        20
                  ....*....|....*....|....*.
gi 1958673202  91 RCVLMGDAAHAIVPFFGQGMNAGFED 116
Cdd:PRK06183  287 RVLLAGDAAHLMPPFAGQGMNSGIRD 312
PRK05714 PRK05714
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 94-149 1.24e-04

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


Pssm-ID: 168201 [Multi-domain]  Cd Length: 405  Bit Score: 43.28  E-value: 1.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958673202  94 LMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFNN------DLSVcLPEFSRFRIPDDHAI 149
Cdd:PRK05714  289 LIGDAAHTIHPLAGQGVNLGFLDAAVLAEVLLHAAErgerlaDVRV-LSRFERRRMPHNLAL 349
PRK08013 PRK08013
oxidoreductase; Provisional
 91-116 1.39e-04

oxidoreductase; Provisional


Pssm-ID: 236139 [Multi-domain]  Cd Length: 400  Bit Score: 43.11  E-value: 1.39e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958673202  91 RCVLMGDAAHAIVPFFGQGMNAGFED 116
Cdd:PRK08013  283 RLALVGDAAHTIHPLAGQGVNLGFMD 308
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
89-116 2.95e-04

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 41.89  E-value: 2.95e-04
                          10        20
                  ....*....|....*....|....*...
gi 1958673202  89 KSRCVLMGDAAHAIVPFFGQGMNAGFED 116
Cdd:PRK07333  279 APRFALVGDAAHGIHPIAGQGLNLGLKD 306
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 87-116 3.00e-04

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: 42.05  E-value: 3.00e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958673202  87 HLKSRCVLMGDAAHAIVPFFGQGMNAGFED 116
Cdd:TIGR01989 330 YVTKRVALVGDAAHRVHPLAGQGVNLGFGD 359
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 89-149 3.49e-04

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: 41.81  E-value: 3.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958673202  89 KSRCVLMGDAAHAIVPFFGQGMNAGFED------CLVFDELMDKFNNDLSVcLPEFSRFRIPDDHAI 149
Cdd:TIGR01988 275 APRLALIGDAAHTIHPLAGQGLNLGLRDvaalaeVLEDARRRGEDIGSLRV-LQRYERRRRFDNAAM 340
PRK06847 PRK06847
hypothetical protein; Provisional
 85-144 3.59e-04

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 41.78  E-value: 3.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673202  85 PFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKfNNDLSVCLPEFSRFRIP 144
Cdd:PRK06847  278 PWH-RGRVVLIGDAAHATTPHLAQGAGMAIEDAIVLAEELAR-HDSLEAALQAYYARRWE 335
PRK06475 PRK06475
FAD-binding protein;
77-144 7.78e-04

FAD-binding protein;


Pssm-ID: 180582 [Multi-domain]  Cd Length: 400  Bit Score: 40.58  E-value: 7.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958673202  77 PMISVKCSPFHLKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDkfNNDLSVCLPEFSRFRIP 144
Cdd:PRK06475  279 PLFEMADAQFVGPDRTIFLGDASHAVTPFAAQGAAMAIEDAAALAEALD--SDDQSAGLKRFDSVRKE 344
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 93-125 1.56e-03

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


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 39.58  E-value: 1.56e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958673202  93 VLMGDAAHAIVPFFGQGMNAGFEDClvfDELMD 125
Cdd:PRK08020  284 ALVGDAAHTINPLAGQGVNLGYRDV---DALLD 313
PRK06126 PRK06126
hypothetical protein; Provisional
 89-116 1.72e-03

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 39.59  E-value: 1.72e-03
                          10        20
                  ....*....|....*....|....*...
gi 1958673202  89 KSRCVLMGDAAHAIVPFFGQGMNAGFED 116
Cdd:PRK06126  302 RGRVFLAGDAAHLFTPTGGYGMNTGIGD 329
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 89-116 1.79e-03

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 39.37  E-value: 1.79e-03
                          10        20
                  ....*....|....*....|....*...
gi 1958673202  89 KSRCVLMGDAAHAIVPFFGQGMNAGFED 116
Cdd:PRK08850  281 RERVALVGDAAHTIHPLAGQGVNLGLLD 308
 
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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