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

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)DescriptionActionsGraphical viewLength
    Binding sitei11Carbamoyl phosphateBy similarity1
    Binding sitei73Carbamoyl phosphate1
    Binding sitei84Carbamoyl phosphate1
    Binding sitei108Carbamoyl phosphate1
    Binding sitei166OrnithineBy similarity1
    Binding sitei230OrnithineBy similarity1
    Binding sitei280Carbamoyl phosphateBy similarity1
    Binding sitei298Carbamoyl phosphateBy similarity1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi22W → A: Decreased heat stability. 1 Publication1
    Mutagenesisi26E → Q: Increased dissociation of dodecamers into trimers. 1 Publication1
    Mutagenesisi30M → A: Increased dissociation of dodecamers into trimers. 1 Publication1
    Mutagenesisi34W → A: Increased dissociation of dodecamers into trimers. 1 Publication1
    Mutagenesisi228Y → C: Becomes active at low temperatures; when associated with G-278. 1 Publication1
    Mutagenesisi241A → D: Becomes active at low temperatures; when associated with G-278. 1 Publication1
    Mutagenesisi278E → G: Becomes active at low temperatures; when associated with C-228 or D-241. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001130732 – 315Ornithine carbamoyltransferaseAdd BLAST314

    Proteomic databases

    PRIDEiQ51742.

    Interactioni

    Subunit structurei

    Homododecamer (tetramer of trimers).2 Publications

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1315
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi13 – 15Combined sources3
    Helixi18 – 37Combined sources20
    Turni43 – 46Combined sources4
    Beta strandi48 – 55Combined sources8
    Helixi59 – 70Combined sources12
    Beta strandi73 – 79Combined sources7
    Helixi80 – 82Combined sources3
    Turni84 – 88Combined sources5
    Helixi91 – 98Combined sources8
    Turni99 – 101Combined sources3
    Beta strandi103 – 108Combined sources6
    Helixi112 – 121Combined sources10
    Beta strandi126 – 130Combined sources5
    Helixi136 – 150Combined sources15
    Beta strandi157 – 162Combined sources6
    Helixi166 – 177Combined sources12
    Beta strandi181 – 185Combined sources5
    Helixi194 – 207Combined sources14
    Beta strandi210 – 215Combined sources6
    Helixi217 – 220Combined sources4
    Turni221 – 223Combined sources3
    Beta strandi225 – 229Combined sources5
    Beta strandi239 – 242Combined sources4
    Helixi243 – 248Combined sources6
    Helixi249 – 251Combined sources3
    Helixi255 – 259Combined sources5
    Beta strandi266 – 269Combined sources4
    Turni276 – 278Combined sources3
    Helixi281 – 284Combined sources4
    Helixi291 – 311Combined sources21

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei32Important for structural integrity1
    Sitei148Important for structural integrity1

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ51742.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni57 – 61Carbamoyl phosphate bindingBy similarity5
    Regioni135 – 138Carbamoyl phosphate bindingBy similarity4
    Regioni234 – 235Ornithine bindingBy similarity2
    Regioni245 – 246Carbamoyl phosphate bindingBy similarity2
    Regioni269 – 272Carbamoyl phosphate bindingBy similarity4

    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.
    OMAiEHPCQIL.

    Family and domain databases

    Gene3Di3.40.50.1370. 2 hits.
    HAMAPiMF_01109. OTCase. 1 hit.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti206E → ER in CAA73260 (PubMed:9288929).Curated1
    Sequence conflicti209Missing in CAA67609 (PubMed:9288929).Curated1

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1A1SX-ray2.70A2-315[»]
    1PVVX-ray1.87A1-315[»]
    ProteinModelPortaliQ51742.
    SMRiQ51742.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-48301N.
    IntActiQ51742. 1 interactor.
    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.
    OMAiEHPCQIL.

    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. 1 hit.
    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...

    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 2, 2016
    This is version 134 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.