Q9MZS9 (KMO_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kynurenine 3-monooxygenase
EC=1.14.13.9

Alternative name(s):
Fpk
Kynurenine 3-hydroxylase

Gene names

Name:

KMO

Organism

Sus scrofa (Pig) [Complete proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract By similarity.
Catalytic activity	L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O.
Cofactor	FAD By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3.
Subcellular location	Mitochondrion outer membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the aromatic-ring hydroxylase family. KMO subfamily.
Sequence caution	The sequence AAF80481.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane Transmembrane helix
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	NAD metabolic process Inferred from sequence or structural similarity. Source: UniProtKB pyridine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	kynurenine 3-monooxygenase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 471	471	Kynurenine 3-monooxygenase		PRO_0000229744
Regions
	Transmembrane	385 – 404	20	Helical; Potential
	Transmembrane	425 – 444	20	Helical; Potential
Amino acid modifications
	Modified residue	399	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9MZS9 [UniParc]. Last modified April 4, 2006. Version 2. Checksum: 0491A30AA441CD16	FASTA	471	53,998
	10 20 30 40 50 60 MDSSDIQRTS IAVIGGGLVG SLNACFLAKR NFQVDVYESR EDIRMAEFAR GRSINLALSY 70 80 90 100 110 120 RGRQALKAIG LEDQIVSQGI PMRARMIHSL SGKKSAIPYG TKSQYILSIS RENLNKDLLT 130 140 150 160 170 180 AVEKYPNAKV HFGHQLLKCR PETGVITLLG PDKVPKDIAC DLILGCDGAY STVRTHLVKK 190 200 210 220 230 240 PRFDYSQQYI PHGYMELTIP PQNGDFAMEP NYLHIWPRDT FMMIALPNMN KSFTCTLFMP 250 260 270 280 290 300 FEEFEKLLTS RDVLDFFQKY FPDSLHLIGK EALAQDFFRL PAQPMISVKC SSFHFNSHCV 310 320 330 340 350 360 LMGDAAHALV PFFGQGMNAG FEDCLVFDEL MDKFNNDFSM CLPEFSKFRI PDDHAISDLS 370 380 390 400 410 420 MYNYIEMRSH VNSRWFIFQK NIERCLHTLM PSTFIPLYTM VTFSRIRYHE AMLRWQWQKK 430 440 450 460 470 VINTALFFFG TLVALSTTYL LTGPTFRSSL GCLRRSWNSV TYFQNIGRIS L

References

[1]	"Purification of L-kynurenine 3-monooxygenase from mitochondrial outer membrane of pig liver." Uemura T., Hirai K. Adv. Exp. Med. Biol. 467:619-623(1999) [PubMed: 10721109] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF163971 mRNA. Translation: AAF80481.1. Different initiation.
RefSeq	NP_999241.1. NM_214076.1.
UniGene	Ssc.283.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397148.
KEGG	ssc:397148.
Organism-specific databases
CTD	8564.
Phylogenomic databases
HOVERGEN	HBG057213.
Family and domain databases
InterPro	IPR002938. mOase_FAD-bd. IPR003042. Rng_hydrolase-like. [Graphical view]
KO	K00486.
Pfam	PF01494. FAD_binding_3. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...

Entry information

Entry name

KMO_PIG

Accession

Primary (citable) accession number: Q9MZS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	April 4, 2006
Last modified:	November 16, 2011
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program