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Protein

Ornithine carbamoyltransferase

Gene

argF

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis.1 Publication

Catalytic activityi

Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline.

Enzyme regulationi

Inhibited by the bisubstrate delta-N-phosphonoacetyl-L-ornithine (PALO).1 Publication

Kineticsi

  1. KM=0.13 mM for L-ornithine2 Publications
  2. KM=0.13 mM for carbamoyl phosphate2 Publications

    pH dependencei

    Optimum pH is 6.5 (at 55 degrees Celsius).2 Publications

    Temperature dependencei

    Extreme thermal stability. It maintains about 50% of its activity after heat treatment for 60 min at 100 degrees Celsius.2 Publications

    Pathwayi: L-arginine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Ornithine carbamoyltransferase (argF)
    2. Argininosuccinate synthase (argG)
    3. Argininosuccinate lyase (argH)
    This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei11 – 111Carbamoyl phosphateBy similarity
    Binding sitei73 – 731Carbamoyl phosphate
    Binding sitei84 – 841Carbamoyl phosphate
    Binding sitei108 – 1081Carbamoyl phosphate
    Binding sitei166 – 1661OrnithineBy similarity
    Binding sitei230 – 2301OrnithineBy similarity
    Binding sitei280 – 2801Carbamoyl phosphateBy similarity
    Binding sitei298 – 2981Carbamoyl phosphateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis

    Enzyme and pathway databases

    BRENDAi2.1.3.3. 5243.
    UniPathwayiUPA00068; UER00112.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ornithine carbamoyltransferase (EC:2.1.3.3)
    Short name:
    OTCase
    Gene namesi
    Name:argF
    Ordered Locus Names:PF0594
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    Proteomesi
    • UP000001013 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 221W → A: Decreased heat stability. 1 Publication
    Mutagenesisi26 – 261E → Q: Increased dissociation of dodecamers into trimers. 1 Publication
    Mutagenesisi30 – 301M → A: Increased dissociation of dodecamers into trimers. 1 Publication
    Mutagenesisi34 – 341W → A: Increased dissociation of dodecamers into trimers. 1 Publication
    Mutagenesisi228 – 2281Y → C: Becomes active at low temperatures; when associated with G-278. 1 Publication
    Mutagenesisi241 – 2411A → D: Becomes active at low temperatures; when associated with G-278. 1 Publication
    Mutagenesisi278 – 2781E → G: Becomes active at low temperatures; when associated with C-228 or D-241. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 315314Ornithine carbamoyltransferasePRO_0000113073Add
    BLAST

    Proteomic databases

    PRIDEiQ51742.

    Interactioni

    Subunit structurei

    Homododecamer (tetramer of trimers).2 Publications

    Protein-protein interaction databases

    DIPiDIP-48301N.
    IntActiQ51742. 1 interaction.
    STRINGi186497.PF0594.

    Structurei

    Secondary structure

    1
    315
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 153Combined sources
    Helixi18 – 3720Combined sources
    Turni43 – 464Combined sources
    Beta strandi48 – 558Combined sources
    Helixi59 – 7012Combined sources
    Beta strandi73 – 797Combined sources
    Helixi80 – 823Combined sources
    Turni84 – 885Combined sources
    Helixi91 – 988Combined sources
    Turni99 – 1013Combined sources
    Beta strandi103 – 1086Combined sources
    Helixi112 – 12110Combined sources
    Beta strandi126 – 1305Combined sources
    Helixi136 – 15015Combined sources
    Beta strandi157 – 1626Combined sources
    Helixi166 – 17712Combined sources
    Beta strandi181 – 1855Combined sources
    Helixi194 – 20714Combined sources
    Beta strandi210 – 2156Combined sources
    Helixi217 – 2204Combined sources
    Turni221 – 2233Combined sources
    Beta strandi225 – 2295Combined sources
    Beta strandi239 – 2424Combined sources
    Helixi243 – 2486Combined sources
    Helixi249 – 2513Combined sources
    Helixi255 – 2595Combined sources
    Beta strandi266 – 2694Combined sources
    Turni276 – 2783Combined sources
    Helixi281 – 2844Combined sources
    Helixi291 – 31121Combined sources

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei32 – 321Important for structural integrity
    Sitei148 – 1481Important for structural integrity

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A1SX-ray2.70A2-315[»]
    1PVVX-ray1.87A1-315[»]
    ProteinModelPortaliQ51742.
    SMRiQ51742. Positions 2-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ51742.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni57 – 615Carbamoyl phosphate bindingBy similarity
    Regioni135 – 1384Carbamoyl phosphate bindingBy similarity
    Regioni234 – 2352Ornithine bindingBy similarity
    Regioni245 – 2462Carbamoyl phosphate bindingBy similarity
    Regioni269 – 2724Carbamoyl phosphate bindingBy similarity

    Domaini

    The monomer folds into two domains of similar size. The N-terminal domain is the carbamoylphosphate-binding domain; ornithine binds to the C-terminal domain.1 Publication

    Sequence similaritiesi

    Belongs to the ATCase/OTCase family.Curated

    Phylogenomic databases

    eggNOGiarCOG00912. Archaea.
    COG0078. LUCA.
    HOGENOMiHOG000022686.
    KOiK00611.
    OMAiGNNMAHS.

    Family and domain databases

    Gene3Di3.40.50.1370. 2 hits.
    HAMAPiMF_01109. OTCase.
    InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    IPR002292. Orn/put_carbamltrans.
    IPR024904. OTCase_ArgI.
    [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.

    Q51742-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVVSLAGRDL LCLQDYTAEE IWTILETAKM FKIWQKIGKP HRLLEGKTLA
    60 70 80 90 100
    MIFQKPSTRT RVSFEVAMAH LGGHALYLNA QDLQLRRGET IADTARVLSR
    110 120 130 140 150
    YVDAIMARVY DHKDVEDLAK YATVPVINGL SDFSHPCQAL ADYMTIWEKK
    160 170 180 190 200
    GTIKGVKVVY VGDGNNVAHS LMIAGTKLGA DVVVATPEGY EPDEKVIKWA
    210 220 230 240 250
    EQNAAESGGS FELLHDPVKA VKDADVIYTD VWASMGQEAE AEERRKIFRP
    260 270 280 290 300
    FQVNKDLVKH AKPDYMFMHC LPAHRGEEVT DDVIDSPNSV VWDQAENRLH
    310
    AQKAVLALVM GGIKF
    Length:315
    Mass (Da):35,181
    Last modified:January 23, 2007 - v6
    Checksum:i14404FBDC2ECCB95
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061E → ER in CAA73260 (PubMed:9288929).Curated
    Sequence conflicti209 – 2091Missing in CAA67609 (PubMed:9288929).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X99225 Genomic DNA. Translation: CAA67609.1.
    Y12727 Genomic DNA. Translation: CAA73260.1.
    AE009950 Genomic DNA. Translation: AAL80718.1.
    PIRiT45077.
    RefSeqiWP_011011713.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL80718; AAL80718; PF0594.
    GeneIDi1468437.
    KEGGipfu:PF0594.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X99225 Genomic DNA. Translation: CAA67609.1.
    Y12727 Genomic DNA. Translation: CAA73260.1.
    AE009950 Genomic DNA. Translation: AAL80718.1.
    PIRiT45077.
    RefSeqiWP_011011713.1. NC_003413.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A1SX-ray2.70A2-315[»]
    1PVVX-ray1.87A1-315[»]
    ProteinModelPortaliQ51742.
    SMRiQ51742. Positions 2-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-48301N.
    IntActiQ51742. 1 interaction.
    STRINGi186497.PF0594.

    Proteomic databases

    PRIDEiQ51742.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL80718; AAL80718; PF0594.
    GeneIDi1468437.
    KEGGipfu:PF0594.

    Phylogenomic databases

    eggNOGiarCOG00912. Archaea.
    COG0078. LUCA.
    HOGENOMiHOG000022686.
    KOiK00611.
    OMAiGNNMAHS.

    Enzyme and pathway databases

    UniPathwayiUPA00068; UER00112.
    BRENDAi2.1.3.3. 5243.

    Miscellaneous databases

    EvolutionaryTraceiQ51742.

    Family and domain databases

    Gene3Di3.40.50.1370. 2 hits.
    HAMAPiMF_01109. OTCase.
    InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    IPR002292. Orn/put_carbamltrans.
    IPR024904. OTCase_ArgI.
    [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

    « Hide 'large scale' publications
    1. "Isolation of the gene encoding Pyrococcus furiosus ornithine carbamoyltransferase and study of its expression profile in vivo and in vitro."
      Roovers M., Hetcke C., Legrain C., Thomm M., Glansdorff N.
      Eur. J. Biochem. 247:1038-1045(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    3. "Biochemical characterisation of ornithine carbamoyltransferase from Pyrococcus furiosus."
      Legrain C., Villeret V., Roovers M., Gigot D., Dideberg O., Pierard A., Glansdorff N.
      Eur. J. Biochem. 247:1046-1055(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-12, FUNCTION AS AN OTCASE, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    4. "Metabolic channeling of carbamoyl phosphate, a thermolabile intermediate: evidence for physical interaction between carbamate kinase-like carbamoyl-phosphate synthetase and ornithine carbamoyltransferase from the hyperthermophile Pyrococcus furiosus."
      Massant J., Verstreken P., Durbecq V., Kholti A., Legrain C., Beeckmans S., Cornelis P., Glansdorff N.
      J. Biol. Chem. 277:18517-18522(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CARBAMOYL-PHOSPHATE SYNTHETASE.
    5. "Experimental evolution of enzyme temperature activity profile: selection in vivo and characterization of low-temperature-adapted mutants of Pyrococcus furiosus ornithine carbamoyltransferase."
      Roovers M., Sanchez R., Legrain C., Glansdorff N.
      J. Bacteriol. 183:1101-1105(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-228; ALA-241 AND GLU-278.
    6. "Probing the role of oligomerization in the high thermal stability of Pyrococcus furiosus ornithine carbamoyltransferase by site-specific mutants."
      Clantin B., Tricot C., Lonhienne T., Stalon V., Villeret V.
      Eur. J. Biochem. 268:3937-3942(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TRP-22; GLU-26; MET-30 AND TRP-34.
    7. "The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures."
      Villeret V., Clantin B., Tricot C., Legrain C., Roovers M., Stalon V., Glansdorff N., van Beeumen J.
      Proc. Natl. Acad. Sci. U.S.A. 95:2801-2806(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SULFATE IONS, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, SUBUNIT.
    8. "Refined structure of Pyrococcus furiosus ornithine carbamoyltransferase at 1.87 A."
      Massant J., Wouters J., Glansdorff N.
      Acta Crystallogr. D 59:2140-2149(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS), SUBUNIT, THERMOSTABILITY.

    Entry informationi

    Entry nameiOTC_PYRFU
    AccessioniPrimary (citable) accession number: Q51742
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: November 11, 2015
    This is version 131 of the entry and version 6 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    It interacts physically with carbamoyl-phosphate synthetase (CKase), forming a channeling cluster for carbamoyl phosphate. This prevents the thermodenaturation of carbamoyl phosphate, an extremely thermolabile and potentially toxic metabolic intermediate (PubMed:9501170).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.