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KMO_CHAGB
ID   KMO_CHAGB               Reviewed;         479 AA.
AC   Q2GQG8;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=Biosynthesis of nicotinic acid protein 4 {ECO:0000255|HAMAP-Rule:MF_03018};
DE   AltName: Full=Kynurenine 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_03018};
GN   Name=BNA4 {ECO:0000255|HAMAP-Rule:MF_03018}; ORFNames=CHGG_09786;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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}.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03018}.
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DR   EMBL; CH408035; EAQ83382.1; -; Genomic_DNA.
DR   RefSeq; XP_001227713.1; XM_001227712.1.
DR   AlphaFoldDB; Q2GQG8; -.
DR   SMR; Q2GQG8; -.
DR   STRING; 38033.XP_001227713.1; -.
DR   EnsemblFungi; EAQ83382; EAQ83382; CHGG_09786.
DR   GeneID; 4397066; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_023210_2_1_1; -.
DR   InParanoid; Q2GQG8; -.
DR   OMA; REFMFIA; -.
DR   OrthoDB; 462247at2759; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
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:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; Mitochondrion outer membrane;
KW   Monooxygenase; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..479
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361925"
SQ   SEQUENCE   479 AA;  53914 MW;  703C8A8F0FD0DE5C CRC64;
     MEKKQKVVVV GAGPVGSLAA LYAANRGDDV EIYELRSDLR DPTTTPLNFT KSINLALSER
     GINAMRHAGQ PKLIEHVMGA TIPMHGRMIH GKRANGDLFE ESQNYDVYGR SILAVDRGRL
     NERLLDILEA MPNVTFFFNH KLTGADFRKN KAWFEVRDKT GAAQGQQSRE IEVKFDLMIG
     TDGAHSAVRY HMMKYTRMDY EQVYIDTMWC EFQIQPKTVV PDAPLDSKFS ISPNHLHIWP
     GKEFMFIAIP SDDGSFTCTL FAPATLYEHL ESDRTGSLVP PFFDKYFPGV TTLIPPTELI
     DSFHRNPHLP LISIKCKPHH YGSSVVILGD AAHAMVPFYG QGMNAGLEDV RILFDILDKH
     ARMDELSACA DRAVSREHAL AEYTAVRVPD AHAINDLALQ NYVEMRASVL SPVYRLRKFL
     EEALSKYVPS LGWQTKYARV SFGNERYSEV VAKSEHQGKM LVRGIGILSC RVGRALHNE
 
 
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