ID C5DE27_LACTC Unreviewed; 463 AA.
AC C5DE27;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Kynurenine 3-monooxygenase {ECO:0000256|HAMAP-Rule:MF_03018};
DE EC=1.14.13.9 {ECO:0000256|HAMAP-Rule:MF_03018};
DE AltName: Full=Biosynthesis of nicotinic acid protein 4 {ECO:0000256|HAMAP-Rule:MF_03018};
DE AltName: Full=Kynurenine 3-hydroxylase {ECO:0000256|HAMAP-Rule:MF_03018};
GN Name=BNA4 {ECO:0000256|HAMAP-Rule:MF_03018};
GN OrderedLocusNames=KLTH0C05786g {ECO:0000313|EMBL:CAR22038.1};
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR22038.1, ECO:0000313|Proteomes:UP000002036};
RN [1] {ECO:0000313|EMBL:CAR22038.1, ECO:0000313|Proteomes:UP000002036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC {ECO:0000313|Proteomes:UP000002036};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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_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:0000256|ARBA:ARBA00000886,
CC ECO:0000256|HAMAP-Rule:MF_03018};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_03018};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 1/3. {ECO:0000256|HAMAP-Rule:MF_03018}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_03018}.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03018}.
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DR EMBL; CU928167; CAR22038.1; -; Genomic_DNA.
DR RefSeq; XP_002552476.1; XM_002552430.1.
DR AlphaFoldDB; C5DE27; -.
DR STRING; 559295.C5DE27; -.
DR GeneID; 8291344; -.
DR KEGG; lth:KLTH0C05786g; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_023210_0_1_1; -.
DR InParanoid; C5DE27; -.
DR OMA; REFMFIA; -.
DR OrthoDB; 2250465at2759; -.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000002036; Chromosome C.
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: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_03018};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_03018};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03018, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03018};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW ECO:0000256|HAMAP-Rule:MF_03018};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_03018};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03018};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03018};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_03018};
KW Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 432..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..360
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 463 AA; 51984 MW; 33F8A26DD32FD09D CRC64;
MPETVAVIGA GLVGCLAAVA LAKRGYEVTL FDYRLDPRLA TTQDRNLRSI NLAISARGIT
SLEYVDKGIS KRVLKDIIPM QGRMIHNLRG HQEAQNYGLF GECINSIDRG VLNNSLLDEV
DNLQNVALKF GHKLSQIKFT PNAKQTCVFT TNAASAAKEY AFDFVLGCDG AYSSTRSQMQ
RELRMDFSQE YIDCCYIELY VPPAKEHNPK FNGKFAISPN HLHIWPRGNY MLIALANGDG
SFTSTFFGPW SLVEGLDTRS KIQDFLTNNF PDAVEIIGLK QAVDAFENHP RGALMCVECS
PYHLSQGRAI ILGDAAHSMV PFYGQGMNCG FEDVRVLMQL LDKHSGNRAA AFEEYSSKRH
TDLVSIIKLA KNNYKEMSHG VISNLYLLRK KLDTLLGRVL KDRWLPLYTM VSFRADIPYH
KAIQIEQRQK KILAYLQAFI LALTSLGGLG LYKVLRRALK NRK
//
