KMO_XENTR
ID KMO_XENTR Reviewed; 473 AA.
AC Q6DIZ8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Kynurenine 3-monooxygenase {ECO:0000255|HAMAP-Rule:MF_03018};
DE EC=1.14.13.9 {ECO:0000255|HAMAP-Rule:MF_03018};
DE AltName: Full=Kynurenine 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_03018};
GN Name=kmo {ECO:0000255|HAMAP-Rule:MF_03018};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form
CC 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic
CC acid. {ECO:0000255|HAMAP-Rule:MF_03018}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine +
CC H2O + NADP(+); Xref=Rhea:RHEA:20545, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57959, ChEBI:CHEBI:58125, ChEBI:CHEBI:58349;
CC EC=1.14.13.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03018};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03018};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03018}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_03018}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03018}.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03018}.
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DR EMBL; BC075387; AAH75387.1; -; mRNA.
DR RefSeq; NP_001006690.1; NM_001006689.1.
DR AlphaFoldDB; Q6DIZ8; -.
DR SMR; Q6DIZ8; -.
DR STRING; 8364.ENSXETP00000035436; -.
DR PaxDb; Q6DIZ8; -.
DR DNASU; 448312; -.
DR Ensembl; ENSXETT00000035436; ENSXETP00000035436; ENSXETG00000016227.
DR GeneID; 448312; -.
DR KEGG; xtr:448312; -.
DR CTD; 8564; -.
DR Xenbase; XB-GENE-966665; kmo.
DR eggNOG; KOG2614; Eukaryota.
DR InParanoid; Q6DIZ8; -.
DR OrthoDB; 462247at2759; -.
DR Reactome; R-XTR-71240; Tryptophan catabolism.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000016227; Expressed in liver and 9 other tissues.
DR ExpressionAtlas; Q6DIZ8; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0004502; F:kynurenine 3-monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; ISS:UniProtKB.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0070189; P:kynurenine metabolic process; IBA:GO_Central.
DR GO; GO:0019674; P:NAD metabolic process; ISS:UniProtKB.
DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_01971; Kynurenine_monooxygenase; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027545; Kynurenine_monooxygenase.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Monooxygenase; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="Kynurenine 3-monooxygenase"
FT /id="PRO_0000229746"
FT TRANSMEM 385..404
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT BINDING 19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 37..40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 85
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT BINDING 99
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT BINDING 111
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 304
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 317..318
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 363
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT BINDING 398
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
SQ SEQUENCE 473 AA; 54261 MW; A0981E438BCB18DC CRC64;
MEIQGNRKKT VSVVGGGLVG SLNACFFAKK GFQVELYEAR EDIRYARMVS GRSINLALSH
RGLQALKAVG LDEKIAAMGI PMRARMIHSV KGRKSSIPYG KQHQYILSVD RANLNKELLS
AAEKYSNVTM HFEHKLRDCN VDSGTMTFLN NMENIIEKKA DLIVGCDGAF SVVRKQFMRK
SRFNYSHVYI PHGYKELTIP PRKGEFAMEP NYLHIWPRNT FMMIALPNLD KSFTCTLFMP
FEDFEKLTTG DQVLDFFKTY FPDSIELIGE KKLTEDFFLL PPQAMISVKC SSFCIDHKCV
IMGDAAHAVV PFYGQGMNAG FEDCLVFSEL MEQYQNNLRI CLHEFSRLRV PDAHAISDLA
MYNYKEMRAH VNSKWFIFRK QVDNILNAIM PTTFIPLYTM VTFSRIRYHE VILRWKWQKK
IINVGLFTVG TTGSVGAAYL VIKYLPFNKY IEHVGNCLTH LKGNAYLSRL WAK
