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Protein

Ornithine carbamoyltransferase chain F

Gene

argF

Organism
Escherichia coli (strain K12)
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.

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.
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Ornithine carbamoyltransferase chain I (argI), Ornithine carbamoyltransferase chain 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 sitei10Carbamoyl phosphateBy similarity1
    Binding sitei72Carbamoyl phosphateBy similarity1
    Binding sitei83Carbamoyl phosphateBy similarity1
    Binding sitei107Carbamoyl phosphateBy similarity1
    Binding sitei168OrnithineBy similarity1
    Binding sitei232OrnithineBy similarity1
    Metal bindingi274ZincBy similarity1
    Binding sitei302Carbamoyl phosphateBy similarity1
    Binding sitei320Carbamoyl phosphateBy similarity1

    GO - Molecular functioni

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:CHAINF-MONOMER.
    ECOL316407:JW0266-MONOMER.
    MetaCyc:CHAINF-MONOMER.
    SABIO-RKP06960.
    UniPathwayiUPA00068; UER00112.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ornithine carbamoyltransferase chain F (EC:2.1.3.3)
    Alternative name(s):
    OTCase-2
    Gene namesi
    Name:argF
    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

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

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

    Proteomic databases

    PaxDbiP06960.
    PRIDEiP06960.

    2D gel databases

    SWISS-2DPAGEP06960.

    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.
    STRINGi511145.b0273.

    Structurei

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei31Important for structural integrityBy similarity1
    Sitei147Important for structural integrityBy similarity1

    3D structure databases

    ProteinModelPortaliP06960.
    SMRiP06960.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni56 – 60Carbamoyl phosphate bindingBy similarity5
    Regioni134 – 137Carbamoyl phosphate bindingBy similarity4
    Regioni236 – 237Ornithine bindingBy similarity2
    Regioni273 – 276Carbamoyl phosphate bindingBy similarity4

    Sequence similaritiesi

    Belongs to the ATCase/OTCase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105DBV. Bacteria.
    COG0078. LUCA.
    HOGENOMiHOG000022686.
    InParanoidiP06960.
    KOiK00611.
    OMAiAAPRELW.
    PhylomeDBiP06960.

    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.

    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.
    PATRICi32115667. VBIEscCol129921_0277.

    Cross-referencesi

    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.

    3D structure databases

    ProteinModelPortaliP06960.
    SMRiP06960.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261491. 11 interactors.
    IntActiP06960. 7 interactors.
    STRINGi511145.b0273.

    2D gel databases

    SWISS-2DPAGEP06960.

    Proteomic databases

    PaxDbiP06960.
    PRIDEiP06960.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73376; AAC73376; b0273.
    BAE76057; BAE76057; BAE76057.
    GeneIDi944844.
    KEGGiecj:JW0266.
    eco:b0273.
    PATRICi32115667. VBIEscCol129921_0277.

    Organism-specific databases

    EchoBASEiEB0065.
    EcoGeneiEG10067. argF.

    Phylogenomic databases

    eggNOGiENOG4105DBV. Bacteria.
    COG0078. LUCA.
    HOGENOMiHOG000022686.
    InParanoidiP06960.
    KOiK00611.
    OMAiAAPRELW.
    PhylomeDBiP06960.

    Enzyme and pathway databases

    UniPathwayiUPA00068; UER00112.
    BioCyciEcoCyc:CHAINF-MONOMER.
    ECOL316407:JW0266-MONOMER.
    MetaCyc:CHAINF-MONOMER.
    SABIO-RKP06960.

    Miscellaneous databases

    PROiP06960.

    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 nameiOTC2_ECOLI
    AccessioniPrimary (citable) accession number: P06960
    Secondary accession number(s): P78308, Q2MCE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 151 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    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

    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.