Kynurenine 3-monooxygenase - Mus musculus (Mouse)

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Regions

Amino acid modifications

Natural variations

Preferred order of sections

Molecule processing

Regions

Amino acid modifications

Natural variations

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

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Q91WN4 (KMO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Protein names

Recommended name:
Kynurenine 3-monooxygenase
EC=1.14.13.9

Alternative name(s):
Kynurenine 3-hydroxylase

Gene names

Name:

Kmo

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Sequence length	479 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. HAMAP-Rule MF_03018
Catalytic activity	L-kynurenine + NADPH + O₂ = 3-hydroxy-L-kynurenine + NADP⁺ + H₂O. HAMAP-Rule MF_03018
Cofactor	FAD By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. HAMAP-Rule MF_03018
Subcellular location	Mitochondrion outer membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_03018.
Sequence similarities	Belongs to the aromatic-ring hydroxylase family. KMO subfamily.

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway NAD metabolic process Inferred from sequence or structural similarity. Source: UniProtKB response to salt stress Inferred from electronic annotation. Source: Compara tryptophan catabolic process to kynurenine Inferred from electronic annotation. Source: Compara
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from direct assay PubMed 12865426. Source: MGI mitochondrial outer membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	NAD(P)H oxidase activity Inferred from electronic annotation. Source: Compara flavin adenine dinucleotide binding Inferred from electronic annotation. Source: Compara kynurenine 3-monooxygenase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 479

479

Kynurenine 3-monooxygenase HAMAP-Rule MF_03018

PRO_0000229743

Transmembrane

385 – 404

Helical; Potential

Transmembrane

425 – 445

Helical; Potential

Modified residue

399

Phosphothreonine Ref.3

Alternative sequence

367 – 400

Missing in isoform 2.

VSP_051974

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: E880997DBC9C8163 Show »	FASTA	479	54,532
10 20 30 40 50 60 MASSDTQGKR VAVIGGGLVG ALNACFLAKR NFQVDVYEAR EDIRVAKSAR GRSINLALSY 70 80 90 100 110 120 RGRQALKAIG LEDQIVSKGV PMKARMIHSL SGKKSAIPYG NKSQYILSIS RENLNKDLLT 130 140 150 160 170 180 AVESYANAKV HFGHKLSKCI PEEGVLTVLG PDKVPRDVTC DLVVGCDGAY STVRAHLMKK 190 200 210 220 230 240 PRFDYTQQYI PHGYMELTIP PKNGEYAMEP NCLHIWPRNA YMMIALPNMD KSFTCTLFMP 250 260 270 280 290 300 FEEFERLPTR SDVLDFFQKN FPDAIPLMGE QALMRDFFLL PAQPMISVKC SPFHLKSHCV 310 320 330 340 350 360 LMGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFNNNLSM CLPEFSRFRI PDDHAISDLS 370 380 390 400 410 420 MYNYIEMRAH VNSRWFLFQK LLDKFLHAIM PSTFIPLYTM VAFTRIRYHE AVLRWHWQKK 430 440 450 460 470 VINRGLFVLG SLIAIGGTYL LVHHLSLRPL EFLRRPAWMG TTGYWTRSTD ISLQVPWSY « Hide
Isoform 2 [UniParc]. Checksum: E2B58D64DDF95BCC Show »	FASTA	445	50,396
10 20 30 40 50 60 MASSDTQGKR VAVIGGGLVG ALNACFLAKR NFQVDVYEAR EDIRVAKSAR GRSINLALSY 70 80 90 100 110 120 RGRQALKAIG LEDQIVSKGV PMKARMIHSL SGKKSAIPYG NKSQYILSIS RENLNKDLLT 130 140 150 160 170 180 AVESYANAKV HFGHKLSKCI PEEGVLTVLG PDKVPRDVTC DLVVGCDGAY STVRAHLMKK 190 200 210 220 230 240 PRFDYTQQYI PHGYMELTIP PKNGEYAMEP NCLHIWPRNA YMMIALPNMD KSFTCTLFMP 250 260 270 280 290 300 FEEFERLPTR SDVLDFFQKN FPDAIPLMGE QALMRDFFLL PAQPMISVKC SPFHLKSHCV 310 320 330 340 350 360 LMGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFNNNLSM CLPEFSRFRI PDDHAISDLS 370 380 390 400 410 420 MYNYIEVAFT RIRYHEAVLR WHWQKKVINR GLFVLGSLIA IGGTYLLVHH LSLRPLEFLR 430 440 RPAWMGTTGY WTRSTDISLQ VPWSY « Hide

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N. Tissue: Liver.
[3]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Sequence databases
EMBL GenBank DDBJ	AK129011 mRNA. No translation available. BC014683 mRNA. Translation: AAH14683.1.
IPI	IPI00128271. IPI00742309.
RefSeq	NP_598570.1. NM_133809.1.
UniGene	Mm.27217.
3D structure databases
ProteinModelPortal	Q91WN4.
SMR	Q91WN4. Positions 8-369.
ModBase	Search...
PTM databases
PhosphoSite	Q91WN4.
Proteomic databases
PaxDb	Q91WN4.
PRIDE	Q91WN4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000040250; ENSMUSP00000038914; ENSMUSG00000039783. ENSMUST00000097458; ENSMUSP00000095067; ENSMUSG00000039783.
GeneID	98256.
KEGG	mmu:98256.
UCSC	uc007dto.1. mouse. uc007dtp.1. mouse.
Organism-specific databases
CTD	8564.
MGI	MGI:2138151. Kmo.
Phylogenomic databases
eggNOG	COG0654.
GeneTree	ENSGT00390000000747.
HOGENOM	HOG000251788.
HOVERGEN	HBG057213.
InParanoid	Q91WN4.
KO	K00486.
OMA	YFPDAIP.
OrthoDB	EOG4WH8KP.
Enzyme and pathway databases
UniPathway	UPA00253; UER00328.
Gene expression databases
ArrayExpress	Q91WN4.
Bgee	Q91WN4.
Genevestigator	Q91WN4.
GermOnline	ENSMUSG00000039783. Mus musculus.
Family and domain databases
HAMAP	MF_01971. Kynurenine_monooxygenase.
InterPro	IPR002938. mOase_FAD-bd. IPR003042. Rng_hydrolase-like. [Graphical view]
Pfam	PF01494. FAD_binding_3. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...
Other
NextBio	353386.
SOURCE	Search...

Entry name

KMO_MOUSE

Accession

Primary (citable) accession number: Q91WN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	December 1, 2001
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q91WN4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q91WN4-2)

The sequence of this isoform differs from the canonical sequence as follows:
367-400: Missing.

Note: No experimental confirmation available.