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Protein

Ornithine carbamoyltransferase, anabolic

Gene

argF

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: -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

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

Catalytic activityi

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

Enzyme regulationi

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

Kineticsi

  1. KM=0.13 mM for L-ornithine1 Publication
  2. KM=0.13 mM for carbamoyl phosphate1 Publication

    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.1 Publication

    Pathwayi: L-arginine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Ornithine carbamoyltransferase, anabolic (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 sitei84Carbamoyl phosphate1 Publication1
    Binding sitei108Carbamoyl phosphateUniRule annotation1
    Binding sitei166OrnithineUniRule annotation1
    Binding sitei230OrnithineUniRule annotation1
    Binding sitei298Carbamoyl phosphateUniRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionTransferase
    Biological processAmino-acid biosynthesis, Arginine biosynthesis

    Enzyme and pathway databases

    BRENDAi2.1.3.3 5243
    UniPathwayiUPA00068; UER00112

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ornithine carbamoyltransferase, anabolic1 Publication (EC:2.1.3.3UniRule annotation)
    Short name:
    OTCase1 Publication
    Gene namesi
    Name:argF1 Publication
    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

    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 carbamoyltransferase, anabolicAdd BLAST314

    Proteomic databases

    PRIDEiQ51742

    Interactioni

    Subunit structurei

    Homododecamer (tetramer of trimers).1 Publication1 Publication

    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

    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 – 60Carbamoyl phosphate bindingUniRule annotation4
    Regioni135 – 138Carbamoyl phosphate bindingUniRule annotation4
    Regioni234 – 235Ornithine bindingUniRule annotation2
    Regioni270 – 271Carbamoyl phosphate bindingUniRule annotation2

    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
    OMAiDGNNVCN
    OrthoDBiPOG093Z05BF

    Family and domain databases

    Gene3Di3.40.50.1370, 3 hits
    HAMAPiMF_01109 OTCase, 1 hit
    InterProiView protein in InterPro
    IPR006132 Asp/Orn_carbamoyltranf_P-bd
    IPR006130 Asp/Orn_carbamoylTrfase
    IPR036901 Asp/Orn_carbamoylTrfase_sf
    IPR006131 Asp_carbamoyltransf_Asp/Orn-bd
    IPR002292 Orn/put_carbamltrans
    IPR024904 OTCase_ArgI
    PfamiView protein in Pfam
    PF00185 OTCace, 1 hit
    PF02729 OTCace_N, 1 hit
    PRINTSiPR00100 AOTCASE
    PR00102 OTCASE
    SUPFAMiSSF53671 SSF53671, 1 hit
    TIGRFAMsiTIGR00658 orni_carb_tr, 1 hit
    PROSITEiView protein in PROSITE
    PS00097 CARBAMOYLTRANSFERASE, 1 hit

    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
    PATRICifig|186497.12.peg.623

    Similar proteinsi

    Entry informationi

    Entry nameiOTCA_PYRFU
    AccessioniPrimary (citable) accession number: Q51742
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: March 28, 2018
    This is version 140 of the entry and version 6 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health