ID   KMO_GRAFK               Reviewed;         447 AA.
AC   A0M4X2;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 80.
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=GFO_2711;
OS   Gramella forsetii (strain KT0803).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gramella.
OX   NCBI_TaxID=411154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT0803;
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAL67667.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CU207366; CAL67667.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041250130.1; NC_008571.1.
DR   AlphaFoldDB; A0M4X2; -.
DR   SMR; A0M4X2; -.
DR   STRING; 411154.GFO_2711; -.
DR   EnsemblBacteria; CAL67667; CAL67667; GFO_2711.
DR   KEGG; gfo:GFO_2711; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_023210_0_1_10; -.
DR   OrthoDB; 504558at2; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000000755; Chromosome.
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..447
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361938"
SQ   SEQUENCE   447 AA;  51750 MW;  950447EE85BBF1C8 CRC64;
     MQKEKDVAIV GSGLVGSLLA IFLRKQGHKV TVFDRRPDVR NVQFSGRSIN LAMSNRGWKA
     LREAGIEDEI RELALPLDKR AMHVEGQSVY FQKYGEEGEA IYSISRGILN RKMIDLAESA
     GATFRFEEKI WDVDMKEARL YTGESEKSVW KEYQFDLIFG ADGAFSRVRH KMQRQSRFNY
     SQHFIDVGYK ELTILANEDG SHKMDNSSFH IWPRGNFMLI AMPNLDGTFT CTLFMPFDGE
     TSFESIKTED EADIFFEKYF PDIKDEISNL KKDFFKNPTS AMVTIKCFPW SYFDKITLVG
     DSAHAIVPFY GQGMNAGFED ISVLNEKMNL YGDDWEKVFE DYQTERKPNA DAIAELSYRN
     FVEMSKKTAD PKFLLRKKIE QKFAENHPDL WTPLYSRVTF SDKAYSDALK IGDYQREIMD
     EVMKIPGIEE KWESSEVEEK IISLIKK