Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Kynurenine 3-monooxygenase

Gene

Kmo

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O.UniRule annotation1 Publication

Cofactori

FADUniRule annotationBy similarity

Kineticsi

  1. KM=11.3 µM for NADPH1 Publication
  2. KM=316 µM for NADH1 Publication

    Pathwayi: NAD(+) biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Kynurenine 3-monooxygenase (Kmo)
    2. Kynureninase (Kynu)
    3. 3-hydroxyanthranilate 3,4-dioxygenase (Haao), 3-hydroxyanthranilate 3,4-dioxygenase (Haao)
    This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    ReactomeiR-RNO-71240. 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:KmoImported
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 13

    Organism-specific databases

    RGDi620610. Kmo.

    Subcellular locationi

    • Mitochondrion outer membrane UniRule annotation1 Publication; Multi-pass membrane protein UniRule annotation1 Publication

    Topology

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

    GO - Cellular componenti

    • extracellular exosome Source: Ensembl
    • integral component of membrane Source: UniProtKB-KW
    • mitochondrial inner membrane Source: Ensembl
    • mitochondrial outer membrane Source: UniProtKB
    • mitochondrion Source: RGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Chemistry

    ChEMBLiCHEMBL3457.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 478478Kynurenine 3-monooxygenaseCuratedPRO_0000229745Add
    BLAST

    Proteomic databases

    PaxDbiO88867.
    PRIDEiO88867.

    PTM databases

    iPTMnetiO88867.
    PhosphoSiteiO88867.

    Expressioni

    Tissue specificityi

    Highest activity in liver and kidney. Low activity in spleen, stomach, intestinal tract, esophagus, heart and lung.1 Publication

    Gene expression databases

    BgeeiENSRNOG00000003709.
    GenevisibleiO88867. RN.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-4580390.
    STRINGi10116.ENSRNOP00000005005.

    Chemistry

    BindingDBiO88867.

    Structurei

    3D structure databases

    ProteinModelPortaliO88867.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG2614. Eukaryota.
    COG0654. LUCA.
    GeneTreeiENSGT00390000000747.
    HOGENOMiHOG000251788.
    HOVERGENiHBG057213.
    InParanoidiO88867.
    KOiK00486.
    OMAiQPMISVK.
    OrthoDBiEOG091G0769.
    PhylomeDBiO88867.
    TreeFamiTF312990.

    Family and domain databases

    Gene3Di3.50.50.60. 2 hits.
    HAMAPiMF_01971. Kynurenine_monooxygenase. 1 hit.
    InterProiIPR002938. FAD-bd.
    IPR023753. FAD/NAD-binding_dom.
    IPR027545. Kynurenine_monooxygenase.
    [Graphical view]
    PfamiPF01494. FAD_binding_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    O88867-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASSDTEGKR VVVIGGGLVG ALNACFLAKR NFQVDVYEAR EDIRVANFMR
    60 70 80 90 100
    GRSINLALSY RGRQALKAVG LEDQIVSKGV PMKARMIHSL SGKKSAIPYG
    110 120 130 140 150
    NKSQYILSIS REKLNKDLLT AVESYPNAKV HFGHKLSKCC PEEGILTMLG
    160 170 180 190 200
    PNKVPRDITC DLIVGCDGAY STVRAHLMKK PRFDYSQQYI PHGYMELTIP
    210 220 230 240 250
    PKNGEYAMEP NCLHIWPRNA FMMIALPNMD KSFTCTLFMS FEEFEKLPTH
    260 270 280 290 300
    SDVLDFFQKN FPDAIPLMGE QALMRDFFLL PAQPMISVKC SPFHLKSRCV
    310 320 330 340 350
    LMGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFNNDLSV CLPEFSRFRI
    360 370 380 390 400
    PDDHAISDLS MYNYIEMRAH VNSRWFLFQR LLDKFLHALM PSTFIPLYTM
    410 420 430 440 450
    VAFTRIRYHE AVLRWHWQKK VINRGLFVLG SLVAIGSAYI LVHHLSPRPL
    460 470
    ELLRSAWTGT SGHWNRSADI SPRVPWSH
    Length:478
    Mass (Da):54,353
    Last modified:November 1, 1998 - v1
    Checksum:i72E775D1C05CFFAB
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF056031 mRNA. Translation: AAC62614.1.
    BC088142 mRNA. Translation: AAH88142.1.
    RefSeqiNP_067604.1. NM_021593.1.
    UniGeneiRn.35029.

    Genome annotation databases

    EnsembliENSRNOT00000005005; ENSRNOP00000005005; ENSRNOG00000003709.
    GeneIDi59113.
    KEGGirno:59113.
    UCSCiRGD:620610. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF056031 mRNA. Translation: AAC62614.1.
    BC088142 mRNA. Translation: AAH88142.1.
    RefSeqiNP_067604.1. NM_021593.1.
    UniGeneiRn.35029.

    3D structure databases

    ProteinModelPortaliO88867.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    MINTiMINT-4580390.
    STRINGi10116.ENSRNOP00000005005.

    Chemistry

    BindingDBiO88867.
    ChEMBLiCHEMBL3457.

    PTM databases

    iPTMnetiO88867.
    PhosphoSiteiO88867.

    Proteomic databases

    PaxDbiO88867.
    PRIDEiO88867.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000005005; ENSRNOP00000005005; ENSRNOG00000003709.
    GeneIDi59113.
    KEGGirno:59113.
    UCSCiRGD:620610. rat.

    Organism-specific databases

    CTDi8564.
    RGDi620610. Kmo.

    Phylogenomic databases

    eggNOGiKOG2614. Eukaryota.
    COG0654. LUCA.
    GeneTreeiENSGT00390000000747.
    HOGENOMiHOG000251788.
    HOVERGENiHBG057213.
    InParanoidiO88867.
    KOiK00486.
    OMAiQPMISVK.
    OrthoDBiEOG091G0769.
    PhylomeDBiO88867.
    TreeFamiTF312990.

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00328.
    ReactomeiR-RNO-71240. Tryptophan catabolism.

    Miscellaneous databases

    PROiO88867.

    Gene expression databases

    BgeeiENSRNOG00000003709.
    GenevisibleiO88867. RN.

    Family and domain databases

    Gene3Di3.50.50.60. 2 hits.
    HAMAPiMF_01971. Kynurenine_monooxygenase. 1 hit.
    InterProiIPR002938. FAD-bd.
    IPR023753. FAD/NAD-binding_dom.
    IPR027545. Kynurenine_monooxygenase.
    [Graphical view]
    PfamiPF01494. FAD_binding_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiKMO_RAT
    AccessioniPrimary (citable) accession number: O88867
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: November 1, 1998
    Last modified: September 7, 2016
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.