Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O15229

- KMO_HUMAN

UniProt

O15229 - KMO_HUMAN

Protein

Kynurenine 3-monooxygenase

Gene

KMO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (20 Feb 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.2 PublicationsUniRule annotation

    Cofactori

    FAD.1 PublicationUniRule annotation

    Kineticsi

    1. KM=24.1 µM for L-kynurenine2 Publications

    Vmax=8.5 µmol/min/mg enzyme2 Publications

    pH dependencei

    Optimum pH is 7.5.2 Publications

    Pathwayi

    GO - Molecular functioni

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

    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-monooxygenaseUniRule annotation (EC:1.14.13.9UniRule annotation)
    Alternative name(s):
    Kynurenine 3-hydroxylaseUniRule annotation
    Gene namesi
    Name:KMOImportedUniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6381. KMO.

    Subcellular locationi

    Mitochondrion outer membrane 1 PublicationUniRule annotation; Multi-pass membrane protein 1 PublicationUniRule annotation

    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

    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-monooxygenaseCuratedPRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei385 – 40420HelicalUniRule annotationAdd
    BLAST
    Transmembranei425 – 44521HelicalUniRule annotationAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aromatic-ring hydroxylase family. KMO subfamily.UniRule annotation

    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.Curated

    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.Curated

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti452 – 4521R → C.2 Publications
    Corresponds to variant rs1053230 [ dbSNP | Ensembl ].
    VAR_030845

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei367 – 40034Missing in isoform 3. 1 PublicationVSP_051972Add
    BLAST
    Alternative sequencei367 – 37913Missing in isoform 2. 1 PublicationVSP_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

    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: LiverImported.
    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: Liver1 Publication.
    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: October 1, 2014
    This is version 119 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