ID M9MAI1_PSEA3 Unreviewed; 1698 AA.
AC M9MAI1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ORFNames=PANT_4d00038 {ECO:0000313|EMBL:GAC71628.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC71628.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(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: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; DF196770; GAC71628.1; -; Genomic_DNA.
DR STRING; 1151754.M9MAI1; -.
DR OrthoDB; 2250465at2759; -.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000011976; 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:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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 InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
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.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000011976};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1656..1677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1165..1585
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 1..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1073..1100
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1698 AA; 182075 MW; 0C37932EC7C2429A CRC64;
MSGATPPGSG TSAQPEQSPS SSGSMPASNS LLDLLAGAPA RVVTSPPTSS FTFSFPAPSR
SASVSSATTI TGTTPTPTTT SVPTDAAVAD SPATMPGSSR KQPQDVSHLM QQFMAPASPL
VILSPNAKSS ESNDPIPSAS PTKQPSAKPQ PAIQNKALQL PPSPPSSVSS ASGPKLRQPS
SGFDSPATSS PSRQNAQLPP MDKDTETPSA PAPAPAPAAS PAVKTPFDFV SPFDMLSSND
DQSADTTPQP SEAQKDSSDA AAKEPLAASV AGYEAAEAGF ARILEKLSAS AAQSKQASER
PEASRPAPEQ PKQEEEPAPA ATSSKSPTRP AFRKLPSVPA HLDTPDKHFH ASRHAAVLKQ
DDAFDQPKSS GLSVLSPSRS SSAPSIATLD LSAQQPGGLS SLTNTKVESS GVALISSPFH
FPCNVSAAGL LPASRIANLG HNVACYAMNK GKVRLIHVAS GARLLVQAPG KAAIRSIAAF
ASSDDDDTFL LAALTERSKE AADEGVVFWR IPASFVVDGK DQDSPILIGR ITADPYKSPF
VYRFTAIAWH PTQPRIAIST SDSNVMVVDI VQQLLHQTQP ASPSKKLRSL SELDVDPDSK
DVAHNEPLCG FAFTPDGAML ATISAPLEGD VSWILGFMPL DRTAGQAKEG DHTFLIKSPL
QEPMIISHLS FITDKQQHIR AALVGFRCNT ILGLYDMDSR AWKHVFKFDG PLHDGDKEHF
NLVQFDAHNS TLLVCNSYRS SIFAVPLDFQ PLPEFDANTS TKTELEARLD QGLLPWGIQL
SYPIKEFALQ DPCTSVSISP DAEAGKPSRL FVVFPEGVSI LRLLVVQPPK DEPAAKSEPA
AEPKPQAKEP EAQPKEEAHA PEPEVVSAPA EVATTPSKSS KKKKKRSKVN AVQAEVPTSE
PQPEVATEDH AHPVEPELEA KDVPAASTAD AVQPTQPPRS AQQPAPVADP VESRPSVSAA
HIDATLSDTV TVAVHDAVAA SVGDGFRHSI ESAIPKEVER LISSTELKAE LTRNIAQTIL
PAVQRTAMEV VNRVLAPHFE DVMMQVSERA ERTIVSEMTS VRKSLVAEQS ESLRDTEKTM
QAMHARMEEM HERIKEMHAR PQPAGRFVEL DESDPASEVE KERRVVPAPV PAQSDAGAVI
STETAPSGAV VPARIPSKCK LPERVAIIGA GPVGCLAALA FAQRGCKVDV FESRPDPRTD
EAVARASQRS INLALSTRGI SGLRSVSLVG LGKYTSDGTD LADLVLQESV PMRARMIHVV
TRRASAGRKA EVREQSQLYS TKGECINSVD RGRLNNILLD HALMHPNVHV HFEHKLQSVD
FDHDSRTAAK KARAGQKQAS GKSTTRASER VKLEFDVHTA NERASRRSVV HLASFVLGCD
GAHSSIRSAM GSLSRMHYTH NYIDTGYVEL SIPPRTSLGA GSRERGDGGL DGKPGGHDAF
ELDPNHLHIW PRHSFMLIAL PNQDGSFTCT LFAPFKMFSK ELATREGIVA FFDEHFPDAL
PLIGADKLVA ALTSRRASAL GSVQCDPYHY KDRAVLIGDA AHAMLPFYGQ GLNCGFEDVR
VLFEMIDSSQ GLEGALEEYT HTRHPDLVAI RQLAENNYRE MAHSVVSWPY LLRKKVDSLL
MAVLPTSMWS SLYAMTTFSD LPYAQVIRTE QRQQRILGHA VASGVLAVLT GAALGVYRTR
GVWQPLTRRW IDSVNTAN
//
