KMO_ASPCL
ID KMO_ASPCL Reviewed; 512 AA.
AC A1CT23;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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; ORFNames=ACLA_081480;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027060; EAW06460.1; -; Genomic_DNA.
DR RefSeq; XP_001267886.1; XM_001267885.1.
DR AlphaFoldDB; A1CT23; -.
DR SMR; A1CT23; -.
DR STRING; 5057.CADACLAP00007392; -.
DR EnsemblFungi; EAW06460; EAW06460; ACLA_081480.
DR GeneID; 4700205; -.
DR KEGG; act:ACLA_081480; -.
DR VEuPathDB; FungiDB:ACLA_081480; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_023210_2_1_1; -.
DR OMA; REFMFIA; -.
DR OrthoDB; 462247at2759; -.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000006701; 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..512
FT /note="Kynurenine 3-monooxygenase"
FT /id="PRO_0000361916"
SQ SEQUENCE 512 AA; 58083 MW; 5B1C7AC98065CD1B CRC64;
MADTVRKPQK VVIVGAGPVG SLAALYAAAR GDEVEVYELR GDLRDPSTIP LNFTKSINLA
LSERGINAMK HSNREELTKN VLRDTIPMYG RMIHGKDRGQ LWEAAQAYDV HGRAINAVDR
STLNNALLDE LEHTPNVKLF FNHKLTGADF RANKAWFERR VPGEAPLPNS ANRVPEIEVD
FDFMLGADGA HSAVRYHMMK FARVDYQQEY IDTLWCEFRI APTENGEFRI SPNHLHIWPG
REFMFIALPS ADKSFTCTLF APAVHYTYLA SSPQKLLDFF DVHFPGVSPE LIPPADLQEQ
FATNPHLPLI SLKCKPHHFG SSVAIVGDAA HAVLPFYGQG LNAGLEDIRV LFEVLDKHSV
YDLDASHEAR REAREKAFQA YTDQRCADTH AINDLSKENY VEMRWGVKTP LYKLRKSIEE
ILDRYVPSLG WQTQYSRVSF SNQRYSDVIK LARRQGTVLG LGLGSTFITA VGVAGYMMWK
NPKQYSPLCF MRYCLRHVSH IWVKFFRNTA YA