KMO_CAEEL
ID KMO_CAEEL Reviewed; 461 AA.
AC Q21795;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
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-1 {ECO:0000255|HAMAP-Rule:MF_03018}; ORFNames=R07B7.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 {ECO:0000255|HAMAP-Rule:MF_03018}.
CC Membrane {ECO:0000255|HAMAP-Rule:MF_03018}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-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; Z75955; CAB00114.1; -; Genomic_DNA.
DR PIR; T24012; T24012.
DR RefSeq; NP_506025.1; NM_073624.3.
DR AlphaFoldDB; Q21795; -.
DR SMR; Q21795; -.
DR BioGRID; 44680; 2.
DR STRING; 6239.R07B7.5; -.
DR EPD; Q21795; -.
DR PaxDb; Q21795; -.
DR PeptideAtlas; Q21795; -.
DR EnsemblMetazoa; R07B7.5.1; R07B7.5.1; WBGene00011089.
DR GeneID; 179657; -.
DR KEGG; cel:CELE_R07B7.5; -.
DR UCSC; R07B7.5; c. elegans.
DR CTD; 179657; -.
DR WormBase; R07B7.5; CE06267; WBGene00011089; kmo-1.
DR eggNOG; KOG2614; Eukaryota.
DR GeneTree; ENSGT00390000000747; -.
DR HOGENOM; CLU_023210_0_1_1; -.
DR InParanoid; Q21795; -.
DR OMA; REFMFIA; -.
DR OrthoDB; 462247at2759; -.
DR PhylomeDB; Q21795; -.
DR Reactome; R-CEL-71240; Tryptophan catabolism.
DR UniPathway; UPA00253; UER00328.
DR PRO; PR:Q21795; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00011089; Expressed in larva and 3 other tissues.
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; IEA:InterPro.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Monooxygenase; NADP;
KW Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..461
FT /note="Kynurenine 3-monooxygenase"
FT /id="PRO_0000361911"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
SQ SEQUENCE 461 AA; 52312 MW; 5521B3A0A15C9E87 CRC64;
MPSVAIAGAG LVGALNACFF AQKGWDVSVY EFRKDIRTMK HVQGRSINLA LSQRGKSALE
AVGLKEYIVN QGVPLYARLI HNKDGKTYSR QPYGKPGEHI VSINRRHLNE VMITQAEKSP
NVKFFFEHKV KNVDYDKKQL VVQCTSQPSK IPTFGNKSPP QEHAEFHVEA DLILACDGAY
SAVRRSLMTI PRFDFSQEYI EHGYVELNIM ANNNEFAFEE NVFHLWPRGH FTLIALANRD
KTFTVTIFAP FSEFEKHMST SEDVLSFFEE NFPDAFLLLG KEHIADTFNR VKPQPLVSIK
CSPHSFFDNL VLMGDAAHAM VPFYGQGMNC GFEDCLVFSE TLEEYGNDIA KAVKVYSDGR
VNDAHSINDL AMYNYEELKD LVNKSSYKLR KKFDTIMNSI FPKSWIPLYS MVTFSRIPYS
EVIERRKRQD KILSRIMTTT STLALIGAAA GIYVNRGKLG L
