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Protein

Ornithine carbamoyltransferase, mitochondrial

Gene

OTC

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline.By similarity1 Publication

Enzyme regulationi

Inhibition by ornithine increases at higher pH.1 Publication

Kineticsi

With an increase in pH, a decrease in KM values for ornithine and an increase in the extent of inhibition by ornithine are observed.

  1. KM=0.11 mM for carbamyl phosphate (at pH 7.5)
  2. KM=1.21 mM for ornithine (at pH 7.5)

    pH dependencei

    Optimum pH is 7.5 in the presence of 5 mM ornithine. The curve shifts toward a more alkaline region with a decrease in ornithine concentration.

    Pathwayi: urea cycle

    This protein is involved in step 1 of the subpathway that synthesizes L-citrulline from L-ornithine and carbamoyl phosphate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Ornithine carbamoyltransferase, mitochondrial (OTC)
    This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-citrulline from L-ornithine and carbamoyl phosphate, the pathway urea cycle and in Nitrogen metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei141 – 1411Carbamoyl phosphateBy similarity
    Binding sitei141 – 1411OrnithineBy similarity
    Binding sitei168 – 1681Carbamoyl phosphateBy similarity
    Binding sitei199 – 1991OrnithineBy similarity
    Active sitei303 – 3031By similarity
    Binding sitei330 – 3301Carbamoyl phosphateBy similarity
    Binding sitei330 – 3301OrnithineBy similarity

    GO - Molecular functioni

    • amino acid binding Source: InterPro
    • ornithine carbamoyltransferase activity Source: UniProtKB

    GO - Biological processi

    • arginine biosynthetic process via ornithine Source: UniProtKB
    • arginine metabolic process Source: Reactome
    • urea cycle Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis, Urea cycle

    Enzyme and pathway databases

    ReactomeiR-GGA-187630. Arginine metabolism.
    SABIO-RKQ9YHY9.
    UniPathwayiUPA00158; UER00271.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ornithine carbamoyltransferase, mitochondrial (EC:2.1.3.3)
    Alternative name(s):
    Ornithine transcarbamylase
    Short name:
    OTCase
    Gene namesi
    Name:OTC
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
    Proteomesi
    • UP000000539 Componenti: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3232MitochondrionBy similarityAdd
    BLAST
    Chaini33 – 354322Ornithine carbamoyltransferase, mitochondrialPRO_0000020337Add
    BLAST

    Post-translational modificationi

    Cleavage of the precursor form to the active form occurs only in the kidney.1 Publication

    Proteomic databases

    PaxDbiQ9YHY9.

    Expressioni

    Tissue specificityi

    Expressed in kidney, brain, heart, liver, pancreas, gizzard, small intestine and breast muscle. More abundant in mitochondrion-rich organs (heart, liver and brain) than in other organs. Activity is only detected in the kidney.1 Publication

    Developmental stagei

    Activity detectable in embryos by day 14. Increases until 7 days post-hatching, then decreases again.1 Publication

    Inductioni

    By diet of egg yolk in animals which have a high level of OTC activity due to presence of OCB gene.1 Publication

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000026160.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9YHY9.
    SMRiQ9YHY9. Positions 35-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni90 – 945Carbamoyl phosphate bindingBy similarity
    Regioni263 – 2675Ornithine bindingBy similarity
    Regioni302 – 3054Ornithine bindingBy similarity

    Sequence similaritiesi

    Belongs to the ATCase/OTCase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG1504. Eukaryota.
    COG0078. LUCA.
    HOGENOMiHOG000022686.
    HOVERGENiHBG007881.
    InParanoidiQ9YHY9.
    KOiK00611.
    PhylomeDBiQ9YHY9.

    Family and domain databases

    Gene3Di3.40.50.1370. 2 hits.
    InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    IPR002292. Orn/put_carbamltrans.
    [Graphical view]
    PfamiPF00185. OTCace. 1 hit.
    PF02729. OTCace_N. 1 hit.
    [Graphical view]
    PRINTSiPR00100. AOTCASE.
    PR00102. OTCASE.
    SUPFAMiSSF53671. SSF53671. 1 hit.
    TIGRFAMsiTIGR00658. orni_carb_tr. 1 hit.
    PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9YHY9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLFNLKNLYR ITKLTQNSKH LPRHFCRGPP NQMNVCLKGR DLLTLQNYTA
    60 70 80 90 100
    DELKYLLWVA SDLKQRIKDK GEYLPLMQGK SLAMIFEKRS TRTRLSAETG
    110 120 130 140 150
    FALLGGHSSF LTKQDIHLGT NESLTDTARV LSSMTNAILA RVYKHNDLDL
    160 170 180 190 200
    MTKEATIPVI NGLSDLYHPL QILADYLTLQ EHYGGLNGLT IAWIGDGNNV
    210 220 230 240 250
    LHSIMTSAAK LGMHLRIATP KGFEPDLRIT KVTEQYSKEY GTRLLLTTDP
    260 270 280 290 300
    LEAANGANVL VTDTWISMGQ EEEKRRRLKA FQGYQITMQT VQSAASNWTF
    310 320 330 340 350
    LHCLPRKPEE VDDEVFYSPR SLVFQEAENR KWTIMAVMVS LLTDYSPQLQ

    MPTF
    Length:354
    Mass (Da):40,245
    Last modified:May 1, 1999 - v1
    Checksum:i20447180BAD9D4ED
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF065629 mRNA. Translation: AAD12234.1.
    AF065638
    , AF065630, AF065631, AF065632, AF065634, AF065635, AF065636, AF065637 Genomic DNA. Translation: AAD33083.1.
    PIRiJE0309.
    RefSeqiNP_990241.1. NM_204910.1.
    UniGeneiGga.434.

    Genome annotation databases

    GeneIDi395735.
    KEGGigga:395735.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF065629 mRNA. Translation: AAD12234.1.
    AF065638
    , AF065630, AF065631, AF065632, AF065634, AF065635, AF065636, AF065637 Genomic DNA. Translation: AAD33083.1.
    PIRiJE0309.
    RefSeqiNP_990241.1. NM_204910.1.
    UniGeneiGga.434.

    3D structure databases

    ProteinModelPortaliQ9YHY9.
    SMRiQ9YHY9. Positions 35-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000026160.

    Proteomic databases

    PaxDbiQ9YHY9.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi395735.
    KEGGigga:395735.

    Organism-specific databases

    CTDi5009.

    Phylogenomic databases

    eggNOGiKOG1504. Eukaryota.
    COG0078. LUCA.
    HOGENOMiHOG000022686.
    HOVERGENiHBG007881.
    InParanoidiQ9YHY9.
    KOiK00611.
    PhylomeDBiQ9YHY9.

    Enzyme and pathway databases

    UniPathwayiUPA00158; UER00271.
    ReactomeiR-GGA-187630. Arginine metabolism.
    SABIO-RKQ9YHY9.

    Miscellaneous databases

    PROiQ9YHY9.

    Family and domain databases

    Gene3Di3.40.50.1370. 2 hits.
    InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    IPR002292. Orn/put_carbamltrans.
    [Graphical view]
    PfamiPF00185. OTCace. 1 hit.
    PF02729. OTCace_N. 1 hit.
    [Graphical view]
    PRINTSiPR00100. AOTCASE.
    PR00102. OTCASE.
    SUPFAMiSSF53671. SSF53671. 1 hit.
    TIGRFAMsiTIGR00658. orni_carb_tr. 1 hit.
    PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Chicken ornithine transcarbamylase gene, structure, regulation, and chromosomal assignment: repetitive sequence motif in intron 3 regulates this enzyme activity."
      Shimogiri T., Kono M., Mannen H., Mizutani M., Tsuji S.
      J. Biochem. 124:962-971(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: White leghorn1 Publication.
      Tissue: Kidney1 Publication.
    2. "Comparison of renal ornithine transcarbamylase activities within different chicken breeds."
      Tsuji S., Fukushima T.
      Biochem. Genet. 19:881-893(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY.
    3. "Genetically controlled quantitative variation of ornithine transcarbamylase in the chick kidney."
      Tsuji S., Nakagawa K., Fukushima T.
      Biochem. Genet. 21:857-869(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME KINETICS.
    4. "Genetic control of ornithine transcarbamylase induction in chick kidney."
      Tsuji S., Nakagawa K., Fukushima T.
      Biochem. Genet. 21:843-855(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENETIC REGULATION.
    5. "Chicken ornithine transcarbamylase: purification and some properties."
      Tsuji S.
      J. Biochem. 94:1307-1315(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME KINETICS, SUBUNIT.
    6. "Induction of ornithine transcarbamylase activity with egg yolk in chick kidney."
      Tsuji S., Nakagawa K., Nomura Y., Mukai F., Fukushima T.
      Poult. Sci. 62:519-524(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, DEVELOPMENTAL STAGE.
    7. "Chicken ornithine transcarbamylase: its unexpected expression."
      Tsuji S., Kanazawa S.
      Biochem. Genet. 25:259-266(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiOTC_CHICK
    AccessioniPrimary (citable) accession number: Q9YHY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 15, 2003
    Last sequence update: May 1, 1999
    Last modified: June 8, 2016
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Ornithine transcarbamylase activity varies within and between different breeds of chicken.

    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.