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O15229

- KMO_HUMAN

UniProt

O15229 - KMO_HUMAN

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Protein
Kynurenine 3-monooxygenase
Gene
KMO
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O.1 Publication

Cofactori

FAD.1 Publication

Kineticsi

  1. KM=24.1 µM for L-kynurenine1 Publication

Vmax=8.5 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Pathwayi

GO - Molecular functioni

  1. NAD(P)H oxidase activity Source: UniProtKB
  2. flavin adenine dinucleotide binding Source: UniProtKB
  3. kynurenine 3-monooxygenase activity Source: UniProtKB

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. kynurenine metabolic process Source: UniProtKB
  5. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  6. response to salt stress Source: UniProtKB
  7. small molecule metabolic process Source: Reactome
  8. tryptophan catabolic process Source: Reactome
  9. tryptophan catabolic process to kynurenine Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS04082-MONOMER.
ReactomeiREACT_916. Tryptophan catabolism.
UniPathwayiUPA00253; UER00328.

Names & Taxonomyi

Protein namesi
Recommended name:
Kynurenine 3-monooxygenase (EC:1.14.13.9)
Alternative name(s):
Kynurenine 3-hydroxylase
Gene namesi
Name:KMO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6381. KMO.

Subcellular locationi

Mitochondrion outer membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei385 – 40420Helical; Reviewed prediction
Add
BLAST
Transmembranei425 – 44521Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of membrane Source: UniProtKB-KW
  4. mitochondrial inner membrane Source: Ensembl
  5. mitochondrial outer membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30172.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Kynurenine 3-monooxygenase
PRO_0000229742Add
BLAST

Proteomic databases

MaxQBiO15229.
PaxDbiO15229.
PRIDEiO15229.

PTM databases

PhosphoSiteiO15229.

Expressioni

Tissue specificityi

Highest levels in placenta and liver. Detectable in kidney.1 Publication

Gene expression databases

ArrayExpressiO15229.
BgeeiO15229.
CleanExiHS_KMO.
GenevestigatoriO15229.

Organism-specific databases

HPAiHPA031115.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000355517.

Structurei

3D structure databases

ProteinModelPortaliO15229.
SMRiO15229. Positions 9-367.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0654.
HOVERGENiHBG057213.
InParanoidiO15229.
KOiK00486.
OMAiQPMISVK.
OrthoDBiEOG7KSX8D.
PhylomeDBiO15229.
TreeFamiTF312990.

Family and domain databases

HAMAPiMF_01971. Kynurenine_monooxygenase.
InterProiIPR027545. Kynurenine_monooxygenase.
IPR002938. mOase_FAD-bd.
IPR003042. Rng_hydrolase-like.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
PRINTSiPR00420. RNGMNOXGNASE.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 12 Publications (identifier: O15229-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MDSSVIQRKK VAVIGGGLVG SLQACFLAKR NFQIDVYEAR EDTRVATFTR    50
GRSINLALSH RGRQALKAVG LEDQIVSQGI PMRARMIHSL SGKKSAIPYG 100
TKSQYILSVS RENLNKDLLT AAEKYPNVKM HFNHRLLKCN PEEGMITVLG 150
SDKVPKDVTC DLIVGCDGAY STVRSHLMKK PRFDYSQQYI PHGYMELTIP 200
PKNGDYAMEP NYLHIWPRNT FMMIALPNMN KSFTCTLFMP FEEFEKLLTS 250
NDVVDFFQKY FPDAIPLIGE KLLVQDFFLL PAQPMISVKC SSFHFKSHCV 300
LLGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFSNDLSL CLPVFSRLRI 350
PDDHAISDLS MYNYIEMRAH VNSSWFIFQK NMERFLHAIM PSTFIPLYTM 400
VTFSRIRYHE AVQRWHWQKK VINKGLFFLG SLIAISSTYL LIHYMSPRSF 450
LRLRRPWNWI AHFRNTTCFP AKAVDSLEQI SNLISR 486
Length:486
Mass (Da):55,810
Last modified:February 20, 2007 - v2
Checksum:i164870D52E62A08A
GO
Isoform 21 Publication (identifier: O15229-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     367-379: Missing.

Note: Gene model based on cDNA data. No experimental confirmation available.

Show »
Length:473
Mass (Da):54,205
Checksum:i9D898B2A91A76782
GO
Isoform 31 Publication (identifier: O15229-3) [UniParc]FASTAAdd to Basket

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

Note: Gene model based on mouse cDNA data. No experimental confirmation available.

Show »
Length:452
Mass (Da):51,682
Checksum:i59D707C5D8F21C03
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti452 – 4521R → C.
Corresponds to variant rs1053230 [ dbSNP | Ensembl ].
VAR_030845

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei367 – 40034Missing in isoform 3. 1 Publication
VSP_051972Add
BLAST
Alternative sequencei367 – 37913Missing in isoform 2. 1 Publication
VSP_051973Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13153 mRNA. Translation: CAA73613.1.
AF056032 mRNA. Translation: AAC62615.1.
AL133390 Genomic DNA. No translation available.
FO393423 Genomic DNA. No translation available.
CCDSiCCDS1618.1. [O15229-1]
RefSeqiNP_003670.2. NM_003679.4. [O15229-1]
UniGeneiHs.731056.
Hs.744065.

Genome annotation databases

EnsembliENST00000366557; ENSP00000355515; ENSG00000117009. [O15229-3]
ENST00000366558; ENSP00000355516; ENSG00000117009. [O15229-2]
ENST00000366559; ENSP00000355517; ENSG00000117009. [O15229-1]
GeneIDi8564.
KEGGihsa:8564.
UCSCiuc001hyy.3. human. [O15229-2]
uc009xgo.2. human. [O15229-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13153 mRNA. Translation: CAA73613.1 .
AF056032 mRNA. Translation: AAC62615.1 .
AL133390 Genomic DNA. No translation available.
FO393423 Genomic DNA. No translation available.
CCDSi CCDS1618.1. [O15229-1 ]
RefSeqi NP_003670.2. NM_003679.4. [O15229-1 ]
UniGenei Hs.731056.
Hs.744065.

3D structure databases

ProteinModelPortali O15229.
SMRi O15229. Positions 9-367.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000355517.

Chemistry

BindingDBi O15229.
ChEMBLi CHEMBL2145.

PTM databases

PhosphoSitei O15229.

Proteomic databases

MaxQBi O15229.
PaxDbi O15229.
PRIDEi O15229.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366557 ; ENSP00000355515 ; ENSG00000117009 . [O15229-3 ]
ENST00000366558 ; ENSP00000355516 ; ENSG00000117009 . [O15229-2 ]
ENST00000366559 ; ENSP00000355517 ; ENSG00000117009 . [O15229-1 ]
GeneIDi 8564.
KEGGi hsa:8564.
UCSCi uc001hyy.3. human. [O15229-2 ]
uc009xgo.2. human. [O15229-1 ]

Organism-specific databases

CTDi 8564.
GeneCardsi GC01P241695.
HGNCi HGNC:6381. KMO.
HPAi HPA031115.
MIMi 603538. gene.
neXtProti NX_O15229.
PharmGKBi PA30172.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0654.
HOVERGENi HBG057213.
InParanoidi O15229.
KOi K00486.
OMAi QPMISVK.
OrthoDBi EOG7KSX8D.
PhylomeDBi O15229.
TreeFami TF312990.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00328 .
BioCyci MetaCyc:HS04082-MONOMER.
Reactomei REACT_916. Tryptophan catabolism.

Miscellaneous databases

GeneWikii KMO_(gene).
GenomeRNAii 8564.
NextBioi 32109.
PROi O15229.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15229.
Bgeei O15229.
CleanExi HS_KMO.
Genevestigatori O15229.

Family and domain databases

HAMAPi MF_01971. Kynurenine_monooxygenase.
InterProi IPR027545. Kynurenine_monooxygenase.
IPR002938. mOase_FAD-bd.
IPR003042. Rng_hydrolase-like.
[Graphical view ]
Pfami PF01494. FAD_binding_3. 1 hit.
[Graphical view ]
PRINTSi PR00420. RNGMNOXGNASE.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional expression of human kynurenine 3-monooxygenase."
    Alberati-Giani D., Cesura A.M., Broger C., Warren W.D., Rover S., Malherbe P.
    FEBS Lett. 410:407-412(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT CYS-452.
    Tissue: Liver.
  2. "Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase."
    Breton J., Avanzi N., Magagnin S., Covini N., Magistrelli G., Cozzi L., Isacchi A.
    Eur. J. Biochem. 267:1092-1099(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, VARIANT CYS-452.
    Tissue: Liver.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Endogenous kynurenines as targets for drug discovery and development."
    Stone T.W., Darlington L.G.
    Nat. Rev. Drug Discov. 1:609-620(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiKMO_HUMAN
AccessioniPrimary (citable) accession number: O15229
Secondary accession number(s): A2A2U8
, A2A2U9, A2A2V0, Q5SY07, Q5SY08, Q5SY09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: February 20, 2007
Last modified: September 3, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Increased in neuroinflammatory conditions. Inhibitors are investigated as potential neuroprotective drugs since they lead to an increased level of kynurenic acid, a neuroprotective NMDA receptor agonist.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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