KMO_PIG
ID KMO_PIG Reviewed; 471 AA.
AC Q9MZS9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
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=Fpk;
DE AltName: Full=Kynurenine 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_03018};
GN Name=KMO {ECO:0000255|HAMAP-Rule:MF_03018};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=10721109; DOI=10.1007/978-1-4615-4709-9_78;
RA Uemura T., Hirai K.;
RT "Purification of L-kynurenine 3-monooxygenase from mitochondrial outer
RT membrane of pig liver.";
RL Adv. Exp. Med. Biol. 467:619-623(1999).
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: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}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03018}.
CC -!- DOMAIN: Transmembrane domains are required for enzymatic activity.
CC {ECO:0000250|UniProtKB:O15229}.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03018}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF80481.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF163971; AAF80481.1; ALT_INIT; mRNA.
DR RefSeq; NP_999241.1; NM_214076.1.
DR AlphaFoldDB; Q9MZS9; -.
DR SMR; Q9MZS9; -.
DR STRING; 9823.ENSSSCP00000021083; -.
DR PaxDb; Q9MZS9; -.
DR PRIDE; Q9MZS9; -.
DR GeneID; 397148; -.
DR KEGG; ssc:397148; -.
DR CTD; 8564; -.
DR eggNOG; KOG2614; Eukaryota.
DR InParanoid; Q9MZS9; -.
DR OrthoDB; 462247at2759; -.
DR BRENDA; 1.14.13.9; 6170.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0004502; F:kynurenine 3-monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; ISS:UniProtKB.
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:0070189; P:kynurenine metabolic process; IBA:GO_Central.
DR GO; GO:0019674; P:NAD metabolic process; ISS:UniProtKB.
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; -; 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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Monooxygenase; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..471
FT /note="Kynurenine 3-monooxygenase"
FT /id="PRO_0000229744"
FT TRANSMEM 385..404
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT BINDING 19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 37..40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 85
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT BINDING 99
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT BINDING 111
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 304
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 317..318
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O15229"
FT BINDING 363
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT BINDING 398
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
SQ SEQUENCE 471 AA; 53998 MW; 0491A30AA441CD16 CRC64;
MDSSDIQRTS IAVIGGGLVG SLNACFLAKR NFQVDVYESR EDIRMAEFAR GRSINLALSY
RGRQALKAIG LEDQIVSQGI PMRARMIHSL SGKKSAIPYG TKSQYILSIS RENLNKDLLT
AVEKYPNAKV HFGHQLLKCR PETGVITLLG PDKVPKDIAC DLILGCDGAY STVRTHLVKK
PRFDYSQQYI PHGYMELTIP PQNGDFAMEP NYLHIWPRDT FMMIALPNMN KSFTCTLFMP
FEEFEKLLTS RDVLDFFQKY FPDSLHLIGK EALAQDFFRL PAQPMISVKC SSFHFNSHCV
LMGDAAHALV PFFGQGMNAG FEDCLVFDEL MDKFNNDFSM CLPEFSKFRI PDDHAISDLS
MYNYIEMRSH VNSRWFIFQK NIERCLHTLM PSTFIPLYTM VTFSRIRYHE AMLRWQWQKK
VINTALFFFG TLVALSTTYL LTGPTFRSSL GCLRRSWNSV TYFQNIGRIS L
