ID E6R1Q0_CRYGW Unreviewed; 506 AA.
AC E6R1Q0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=CGB_C6220W {ECO:0000313|EMBL:ADV21140.1};
OS Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus gattii species complex.
OX NCBI_TaxID=367775 {ECO:0000313|EMBL:ADV21140.1, ECO:0000313|Proteomes:UP000007805};
RN [1] {ECO:0000313|EMBL:ADV21140.1, ECO:0000313|Proteomes:UP000007805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM276 / ATCC MYA-4071 {ECO:0000313|Proteomes:UP000007805};
RX PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 2:E342-E342(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WM276;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwong-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 0:0-0(2011).
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; CP000288; ADV21140.1; -; Genomic_DNA.
DR RefSeq; XP_003192927.1; XM_003192879.1.
DR AlphaFoldDB; E6R1Q0; -.
DR GeneID; 10187726; -.
DR KEGG; cgi:CGB_C6220W; -.
DR VEuPathDB; FungiDB:CGB_C6220W; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_023210_0_1_1; -.
DR OrthoDB; 2250465at2759; -.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000007805; 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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 478..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..353
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 153..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 506 AA; 56752 MW; A235E31317AA1CB2 CRC64;
MPQSRARKAL IVGAGPVGAL TALSLHRRGW EVEVWESRDD PRCQDAAPSN LRSINLAISS
RGLEALRSVD PSIAENFLEE AIPMKGRMIH HTDGRQESQL YDPIGGQSIN SISRPILNQR
LVQSLPEEIK LRFNTKLNHI DFKNRVAYAS HKQGATVMPG EESVEDKKQN TENEDGTAFD
LVIGCDGSWS KVRNAMMRVE RIDFSQSFIP HAYIELHMPS NPALPGGYAM NKNHLHIWPR
HAFMLIGLPN KDGSFTLTLF IPFSSLELIT TRESAAAFFK ENFPSAVEIV GEKVLLDDFE
KNPRGNLVTI NCTPSTWSSH AILLGDASHS MVPFYGQGLN CGLEDVRVLN SILERHHISP
TTTRALGETD PELELALKAY SDERQGDLKA ICELALQNYT EMRSHVLSPL HHLRRQVDKI
MTTLFRSTPQ ATLSLTEPFP TKRVRGWTSL YEMVTFRPDV GYSEALRKER WQKDVVGYTG
WIGSVIGISA AGVFAVTMAK KWLERR
//
