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 subunit F

Gene

argF

Organism
Escherichia coli (strain K12)
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

ArgF might be the product of a relatively recent event (duplication or transposition) peculiar to E.coli strain K-12.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=0.02 mM for carbamoyl phosphate1 Publication
  2. KM=5 mM for L-ornithine1 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.Curated
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Ornithine carbamoyltransferase subunit I (argI), Ornithine carbamoyltransferase subunit F (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 sitei83Carbamoyl phosphateUniRule annotation1
    Binding sitei107Carbamoyl phosphateUniRule annotation1
    Binding sitei168OrnithineUniRule annotation1
    Binding sitei232OrnithineUniRule annotation1
    Binding sitei320Carbamoyl phosphateUniRule annotation1

    GO - Molecular functioni

    • amino acid binding Source: InterPro
    • metal ion binding Source: UniProtKB-KW
    • ornithine carbamoyltransferase activity Source: EcoCyc

    GO - Biological processi

    Keywordsi

    Molecular functionTransferase
    Biological processAmino-acid biosynthesis, Arginine biosynthesis
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:CHAINF-MONOMER
    MetaCyc:CHAINF-MONOMER
    SABIO-RKiP06960
    UniPathwayiUPA00068; UER00112

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ornithine carbamoyltransferase subunit F1 Publication (EC:2.1.3.3UniRule annotation)
    Short name:
    OTCase-21 Publication
    Gene namesi
    Name:argF1 Publication
    Ordered Locus Names:b0273, JW0266
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10067 argF

    Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001129192 – 334Ornithine carbamoyltransferase subunit FAdd BLAST333

    Proteomic databases

    PaxDbiP06960
    PRIDEiP06960

    2D gel databases

    SWISS-2DPAGEiP06960

    Interactioni

    Subunit structurei

    In E.coli strain K12, trimer of identical or non-identical chains are composed of ArgI (I) and/or ArgF (F). The trimer has the following composition: FFI, FFF, FII, III. E.coli strains B and W, which are known to contain only ArgI, produce only a trimer of identical chains (III).2 Publications

    Protein-protein interaction databases

    BioGridi4261491, 11 interactors
    IntActiP06960, 7 interactors
    STRINGi316385.ECDH10B_0261

    Structurei

    3D structure databases

    ProteinModelPortaliP06960
    SMRiP06960
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni56 – 59Carbamoyl phosphate bindingUniRule annotation4
    Regioni134 – 137Carbamoyl phosphate bindingUniRule annotation4
    Regioni236 – 237Ornithine bindingUniRule annotation2
    Regioni274 – 275Carbamoyl phosphate bindingUniRule annotation2

    Sequence similaritiesi

    Belongs to the ATCase/OTCase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105DBV Bacteria
    COG0078 LUCA
    HOGENOMiHOG000022686
    InParanoidiP06960
    KOiK00611
    OMAiNLSRWCD
    PhylomeDBiP06960

    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.

    P06960-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSDLYKKHFL KLLDFTPAQF TSLLTLAAQL KADKKNGKEV QKLTGKNIAL
    60 70 80 90 100
    IFEKDSTRTR CSFEVAAFDQ GARVTYLGPS GSQIGHKESI KDTARVLGRM
    110 120 130 140 150
    YDGIQYRGHG QEVVETLAQY AGVPVWNGLT NEFHPTQLLA DLMTMQEHLP
    160 170 180 190 200
    GKAFNEMTLV YAGDARNNMG NSMLEAAALT GLDLRLLAPK ACWPEESLVA
    210 220 230 240 250
    ECSALAEKHG GKITLTEDVA AGVKGADFIY TDVWVSMGEA KEKWAERIAL
    260 270 280 290 300
    LRGYQVNAQM MALTDNPNVK FLHCLPAFHD DQTTLGKQMA KEFDLHGGME
    310 320 330
    VTDEVFESAA SIVFDQAENR MHTIKAVMMA TLGE
    Length:334
    Mass (Da):36,827
    Last modified:January 23, 2007 - v4
    Checksum:iC1EA07CD2AFC39C4
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti121A → P in CAA25329 (PubMed:6382166).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X00759 Genomic DNA Translation: CAA25329.1
    U70214 Genomic DNA Translation: AAB08694.1
    U00096 Genomic DNA Translation: AAC73376.1
    AP009048 Genomic DNA Translation: BAE76057.1
    PIRiA64753 OWECF
    RefSeqiNP_414807.1, NC_000913.3
    WP_001281825.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC73376; AAC73376; b0273
    BAE76057; BAE76057; BAE76057
    GeneIDi944844
    KEGGiecj:JW0266
    eco:b0273
    PATRICifig|1411691.4.peg.2007

    Similar proteinsi

    Entry informationi

    Entry nameiOTC2_ECOLI
    AccessioniPrimary (citable) accession number: P06960
    Secondary accession number(s): P78308, Q2MCE9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: March 28, 2018
    This is version 159 of the entry and version 4 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health