KMO_ASHGO
ID KMO_ASHGO Reviewed; 466 AA.
AC Q751I2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 114.
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}; OrderedLocusNames=AGL276W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54215.1; -; Genomic_DNA.
DR RefSeq; NP_986391.1; NM_211453.1.
DR AlphaFoldDB; Q751I2; -.
DR SMR; Q751I2; -.
DR STRING; 33169.AAS54215; -.
DR EnsemblFungi; AAS54215; AAS54215; AGOS_AGL276W.
DR GeneID; 4622684; -.
DR KEGG; ago:AGOS_AGL276W; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_023210_0_1_1; -.
DR InParanoid; Q751I2; -.
DR OMA; REFMFIA; -.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:EnsemblFungi.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0004502; F:kynurenine 3-monooxygenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; Mitochondrion outer membrane;
KW Monooxygenase; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW Reference proteome.
FT CHAIN 1..466
FT /note="Kynurenine 3-monooxygenase"
FT /id="PRO_0000361915"
SQ SEQUENCE 466 AA; 52142 MW; 5D79B03EA4BE8D9B CRC64;
MGEKGESVAV IGAGLVGCLA ALAFAKKGYE VSLFDYRSDP RLATTTDRNL RSINLAISAR
GIEGLKAVDD ELAARVLRDM LPMHGRMIHN LAGKQEPQEY GLFGESVNSI DRGVLNNALL
DEVSAQEHIQ AQFGHKLVKA NFNHGATQQL LFAVEGKTVQ LEFDFVVGCD GAYSTTRQQM
QRFDRMDFSQ EYMDCFYLEL YIPPTPEFSE RFGGPFAISP QHLHIWPRHN FMLIALPNKD
GSFTSTFFGP WSLLDRLDTR EQLAAFLTTN FADAMELIGL DNAIRAFQEN TKGALMCVEC
RPYHLPGGKA ILLGDAAHAM VPFYGQGMNC GFEDVRVLMG LLDDYAGDRT AAFAKYTASR
HRDLVSIIQL AKNNYRDMSH NVVSSWHRAK RSLNNVLGRT FRGTWLPLYT MVSFRADIPY
HKAVEVDRRQ AAILSLVQSA LLSLAALGGF KGLLLLYRWI KQVRRV
