ID   KMO_SALAI               Reviewed;         454 AA.
AC   A8LVF4;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Kynurenine 3-monooxygenase {ECO:0000255|HAMAP-Rule:MF_01971};
DE            EC=1.14.13.9 {ECO:0000255|HAMAP-Rule:MF_01971};
DE   AltName: Full=Kynurenine 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_01971};
GN   Name=kmo {ECO:0000255|HAMAP-Rule:MF_01971}; OrderedLocusNames=Sare_4893;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) 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_01971}.
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_01971};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01971};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_01971}.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01971}.
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DR   EMBL; CP000850; ABW00643.1; -; Genomic_DNA.
DR   RefSeq; WP_012184866.1; NC_009953.1.
DR   AlphaFoldDB; A8LVF4; -.
DR   SMR; A8LVF4; -.
DR   STRING; 391037.Sare_4893; -.
DR   EnsemblBacteria; ABW00643; ABW00643; Sare_4893.
DR   GeneID; 5707545; -.
DR   KEGG; saq:Sare_4893; -.
DR   PATRIC; fig|391037.6.peg.4940; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_023210_0_1_11; -.
DR   OMA; EALHVWP; -.
DR   OrthoDB; 504558at2; -.
DR   UniPathway; UPA00253; UER00328.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004502; F:kynurenine 3-monooxygenase activity; IEA:UniProtKB-UniRule.
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: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; Monooxygenase; NADP; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN           1..454
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361943"
SQ   SEQUENCE   454 AA;  49556 MW;  99AE6CB347EFF8C5 CRC64;
     MNRRRERVVV VGAGLAGSLA ALYLARQGHE VDIFERRPDP RSALAGPEGR SINLGLSARG
     MRALDGVGLL ADVLKHSVPM RDRVVHSPDG GVRAQPYGVR EHEILHSVLR EELISLVVSA
     AEAEPGVRFH FDSLLTSLDR ETGTVRVAPT AGGEASTVTA DLVVGADGVF STVRQQMQHG
     LRANYAQDFL PWGYKELTIP VGTDGQPRVR LEALHVWPGH EALMVAHPNR DGSLTCTLFM
     AHEGPVSFAA LDTPAAVRDF FRRRFPDAEE LMPDLVREIT EHPVGHLVTV RTAPWRYADR
     VVLIGDAAHA VYPFYGQGMN SAFEDCVVLD ECLTAHPDRA AALAAYEAAR KPHTDVLADL
     STANFEDLRD RVHRLGYSAS AAADRLLARL LPQRWVPLYA MVAHTTIPYA DALARANRQD
     RILRRAGAGL TLAVGLAATA AALRVGRRRR AARR