ID   A4ATE1_MARSH            Unreviewed;       447 AA.
AC   A4ATE1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Kynurenine 3-monooxygenase {ECO:0000256|HAMAP-Rule:MF_01971};
DE            EC=1.14.13.9 {ECO:0000256|HAMAP-Rule:MF_01971};
DE   AltName: Full=Kynurenine 3-hydroxylase {ECO:0000256|HAMAP-Rule:MF_01971};
GN   Name=kmo {ECO:0000256|HAMAP-Rule:MF_01971};
GN   OrderedLocusNames=FB2170_16541 {ECO:0000313|EMBL:EAR00711.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00711.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00711.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the genus
RT   Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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:0000256|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:0000256|ARBA:ARBA00000886,
CC         ECO:0000256|HAMAP-Rule:MF_01971};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974, ECO:0000256|HAMAP-
CC         Rule:MF_01971};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 1/3. {ECO:0000256|HAMAP-Rule:MF_01971}.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01971}.
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DR   EMBL; CP002157; EAR00711.1; -; Genomic_DNA.
DR   RefSeq; WP_013304514.1; NC_014472.1.
DR   AlphaFoldDB; A4ATE1; -.
DR   STRING; 313603.FB2170_16541; -.
DR   KEGG; fbc:FB2170_16541; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_023210_0_1_10; -.
DR   OrthoDB; 9766816at2; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; FAD/NAD(P)-binding domain; 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   PANTHER; PTHR46028; KYNURENINE 3-MONOOXYGENASE; 1.
DR   PANTHER; PTHR46028:SF2; KYNURENINE 3-MONOOXYGENASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01971};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01971}; Membrane {ECO:0000256|SAM:Phobius};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW   Rule:MF_01971};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01971};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01971};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|HAMAP-Rule:MF_01971};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..356
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   447 AA;  51706 MW;  C9FE092A7DF82B8C CRC64;
     MSQTSKNIAI VGSGLVGSLL AIYLRKLGHA ITVFDRRPDI RTIEFSGRSI NLAMSNRGWR
     ALDEIGIEEE IKKIAIPLDK RAMHVVGKPM YFQHYGEEGE AIWSISRGVL NRKMIDLAEE
     AGVKFKFEEK VWDVDLPAAK LQTGETEKGE WKEYAYDLIF GCDGAFSRIR HKMQRRSRFD
     YSQDFIDVGY KELTIPANSD GSHKLDANSF HIWPRGRFMF IAMPNIDGSF TCTLFMPFEG
     DISFESIRTH EEARTFFRTH FPSVDQEIEN LAHDFFKNPT SAMVTMKCYP WTYWDKVALV
     GDSAHAIVPF YGQGMNAGFE DIFVLNKIIK EEGDNWEAIF QQYQKKRKPN ADAIAELSYR
     NFMEMSSKTA DPKFLMQKKI EKRFAQKYPD KWVPLYSRVT FSHRPYSEAL AIGNAQEKIM
     SQIMDFPDIE KKWDSDEIEQ EILNMLP
//