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Q91WN4 (KMO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynurenine 3-monooxygenase

EC=1.14.13.9
Alternative name(s):
Kynurenine 3-hydroxylase
Gene names
Name:Kmo
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence 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. HAMAP-Rule MF_03018

Catalytic activity

L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O. HAMAP-Rule MF_03018

Cofactor

FAD By similarity. HAMAP-Rule MF_03018

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.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

NAD metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

quinolinate biosynthetic process

Inferred from electronic annotation. Source: InterPro

response to salt stress

Inferred from electronic annotation. Source: Ensembl

tryptophan catabolic process to kynurenine

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentintegral component of 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

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

   Molecular_functionNAD(P)H oxidase activity

Inferred from electronic annotation. Source: Ensembl

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: Ensembl

kynurenine 3-monooxygenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Kynurenine 3-monooxygenase HAMAP-Rule MF_03018
PRO_0000229743

Regions

Transmembrane385 – 40420Helical; Potential
Transmembrane425 – 44521Helical; Potential

Natural variations

Alternative sequence367 – 40034Missing in isoform 2.
VSP_051974

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: E880997DBC9C8163

FASTA47954,532
        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 »

FASTA44550,396

References

[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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK129011 mRNA. No translation available.
BC014683 mRNA. Translation: AAH14683.1.
RefSeqNP_598570.1. NM_133809.1.
UniGeneMm.27217.

3D structure databases

ProteinModelPortalQ91WN4.
SMRQ91WN4. Positions 7-367.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ91WN4.

Proteomic databases

PaxDbQ91WN4.
PRIDEQ91WN4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040250; ENSMUSP00000038914; ENSMUSG00000039783. [Q91WN4-1]
ENSMUST00000097458; ENSMUSP00000095067; ENSMUSG00000039783. [Q91WN4-2]
GeneID98256.
KEGGmmu:98256.
UCSCuc007dto.1. mouse. [Q91WN4-1]
uc011wxd.1. mouse. [Q91WN4-2]

Organism-specific databases

CTD8564.
MGIMGI:2138151. Kmo.

Phylogenomic databases

eggNOGCOG0654.
GeneTreeENSGT00390000000747.
HOGENOMHOG000251788.
HOVERGENHBG057213.
InParanoidQ91WN4.
KOK00486.
OMAQPMISVK.
PhylomeDBQ91WN4.
TreeFamTF312990.

Enzyme and pathway databases

UniPathwayUPA00253; UER00328.

Gene expression databases

ArrayExpressQ91WN4.
BgeeQ91WN4.
GenevestigatorQ91WN4.

Family and domain databases

HAMAPMF_01971. Kynurenine_monooxygenase.
InterProIPR027545. Kynurenine_monooxygenase.
IPR002938. mOase_FAD-bd.
IPR003042. Rng_hydrolase-like.
[Graphical view]
PfamPF01494. FAD_binding_3. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
ProtoNetSearch...

Other

NextBio353386.
PROQ91WN4.
SOURCESearch...

Entry information

Entry nameKMO_MOUSE
AccessionPrimary (citable) accession number: Q91WN4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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