ID A0A2K5HWQ7_COLAP Unreviewed; 485 AA.
AC A0A2K5HWQ7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=Kynurenine 3-hydroxylase {ECO:0000256|HAMAP-Rule:MF_03018};
GN Name=KMO {ECO:0000256|HAMAP-Rule:MF_03018};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000008780.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000008780.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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, a neurotoxic NMDA receptor antagonist and potential endogenous
CC inhibitor of NMDA receptor signaling in axonal targeting,
CC synaptogenesis and apoptosis during brain development. Quinolinic acid
CC may also affect NMDA receptor signaling in pancreatic beta cells,
CC osteoblasts, myocardial cells, and the gastrointestinal tract.
CC {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}; Multi-pass membrane protein {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 AlphaFoldDB; A0A2K5HWQ7; -.
DR STRING; 336983.ENSCANP00000008780; -.
DR Ensembl; ENSCANT00000031646.1; ENSCANP00000008780.1; ENSCANG00000027790.1.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000233080; Unplaced.
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|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:UP000233080};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 382..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..324
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 485 AA; 55804 MW; 814FCC67336ED183 CRC64;
MDSSVIQRKK VAVIGGGLVG SLQACFLAKR NFQIDVYEAR EDPRVADFTR GRSINLALSH
RGRQALKAVG LEDQIVAQGI PMRARMIHSL SGKKSAVPYG TKSQYILSVS RENLNKDLLT
AAEKYPSVKM HFNHKLLKCN PEEGMITVLG SNKVPKDVTC DLIVGCDGAY STVRSHLMKK
PRFDYSQQYI PHGYMELTIP PRNGDYAMEP NYLHIWPRNT FMMIALPNMS KSFTCTLFMP
FEEYDKLLTS NDVIDFFQKY FPDAIPLIGE KLLVQDFFLL PAQPMISVKC SSFHFQSHCV
LLGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFNNDLSL CLPAFSRLRI PDSHAISDLS
MYNYIEMRAH VNSSWFIFQK KMWGFLHAIM PSTFIPLYTM VSFSRIRYHE AVQRWHWQKK
VIHKGLFFLG SLIAISSTYL LMHYMSPRPF HYLRRPWNWI AHFWNTTCFP TKAMDSLEQT
YLISR
//
