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Protein

Putrescine carbamoyltransferase

Gene

ptcA

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorolysis of N-carbamoylputrescine to form carbamoyl phosphate and putrescine. Is involved in the degradation pathway of the polyamine agmatine. Also has weak activity with ornithine and cadaverine.1 Publication

Catalytic activityi

Carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine.1 Publication

Enzyme regulationi

Inhibited by spermidine and N-(phosphonoacetyl)-putrescine.2 Publications

Kineticsi

  1. KM=58 µM for carbamoyl phosphate1 Publication
  2. KM=2.3 mM for putrescine1 Publication

    pH dependencei

    Optimum pH is 6.7 with 10 mM putrescine and 10 mM carbamoyl phosphate, 7.8 with 0.2 mM putrescine and 0.2 mM carbamoyl phosphate, and 9.0 with 0.5 mM putrescine and 10 mM carbamoyl phosphate.1 Publication

    Pathway: putrescine biosynthesis via agmatine pathway

    This protein is involved in step 1 of the subpathway that synthesizes putrescine from N-carbamoylputrescine (transferase route).
    Proteins known to be involved in this subpathway in this organism are:
    1. Putrescine carbamoyltransferase (ptcA)
    This subpathway is part of the pathway putrescine biosynthesis via agmatine pathway, which is itself part of Amine and polyamine biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes putrescine from N-carbamoylputrescine (transferase route), the pathway putrescine biosynthesis via agmatine pathway and in Amine and polyamine biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei27 – 271Important for structural integrityBy similarity
    Binding sitei103 – 1031Carbamoyl phosphateBy similarity
    Binding sitei130 – 1301Carbamoyl phosphateBy similarity
    Sitei143 – 1431Important for structural integrityBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Polyamine biosynthesis

    Enzyme and pathway databases

    BioCyciEFAE226185:GHI1-718-MONOMER.
    BRENDAi2.1.3.3. 2095.
    2.1.3.6. 2095.
    SABIO-RKQ837U7.
    UniPathwayiUPA00534; UER00941.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putrescine carbamoyltransferase (EC:2.1.3.6)
    Short name:
    PTC
    Short name:
    PTCase
    Alternative name(s):
    Agmatine catabolism protein B
    Putrescine transcarbamoylase
    Putrescine transcarbamylase
    Gene namesi
    Name:ptcA
    Synonyms:agcB, argF-2
    Ordered Locus Names:EF_0732
    OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
    Taxonomic identifieri226185 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
    ProteomesiUP000001415 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 339339Putrescine carbamoyltransferasePRO_0000112923Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.2 Publications

    Protein-protein interaction databases

    STRINGi226185.EF0732.

    Structurei

    Secondary structure

    1
    339
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 103Combined sources
    Helixi13 – 3119Combined sources
    Turni38 – 414Combined sources
    Beta strandi43 – 508Combined sources
    Helixi54 – 6512Combined sources
    Beta strandi69 – 735Combined sources
    Turni75 – 773Combined sources
    Beta strandi80 – 845Combined sources
    Helixi86 – 9611Combined sources
    Beta strandi98 – 1036Combined sources
    Helixi107 – 11610Combined sources
    Beta strandi121 – 1233Combined sources
    Helixi131 – 14313Combined sources
    Helixi151 – 1533Combined sources
    Beta strandi155 – 1617Combined sources
    Helixi164 – 17512Combined sources
    Beta strandi179 – 1835Combined sources
    Helixi186 – 1883Combined sources
    Helixi192 – 20514Combined sources
    Beta strandi208 – 2125Combined sources
    Helixi215 – 2184Combined sources
    Beta strandi222 – 2265Combined sources
    Beta strandi229 – 2324Combined sources
    Helixi239 – 2468Combined sources
    Turni247 – 2504Combined sources
    Helixi254 – 2607Combined sources
    Beta strandi265 – 2684Combined sources
    Turni275 – 2773Combined sources
    Helixi280 – 2834Combined sources
    Helixi290 – 31526Combined sources
    Helixi320 – 33617Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3TXXX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L1-339[»]
    4A8HX-ray2.50A/B1-339[»]
    4A8PX-ray2.00A/B/C/D/E/F1-339[»]
    4A8TX-ray1.59A1-317[»]
    4AM8X-ray1.99A/B/C/D/E/F1-339[»]
    ProteinModelPortaliQ837U7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 565Carbamoyl phosphate bindingBy similarity
    Regioni268 – 2714Putrescine bindingBy similarity

    Sequence similaritiesi

    Belongs to the ATCase/OTCase family. PTCase subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0078.
    KOiK13252.
    OMAiMGMDFVQ.
    OrthoDBiEOG690MGV.

    Family and domain databases

    Gene3Di3.40.50.1370. 2 hits.
    HAMAPiMF_02102. PTCase.
    InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    IPR002292. Orn/put_carbamltrans.
    IPR024903. PtcA.
    [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.
    TIGR04384. putr_carbamoyl. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q837U7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKRDYVTTET YTKEEMHYLV DLSLKIKEAI KNGYYPQLLK NKSLGMIFQQ
    60 70 80 90 100
    SSTRTRVSFE TAMEQLGGHG EYLAPGQIQL GGHETIEDTS RVLSRLVDIL
    110 120 130 140 150
    MARVERHHSI VDLANCATIP VINGMSDYNH PTQELGDLCT MVEHLPEGKK
    160 170 180 190 200
    LEDCKVVFVG DATQVCFSLG LITTKMGMNF VHFGPEGFQL NEEHQAKLAK
    210 220 230 240 250
    NCEVSGGSFL VTDDASSVEG ADFLYTDVWY GLYEAELSEE ERMKVFYPKY
    260 270 280 290 300
    QVNQEMMDRA GANCKFMHCL PATRGEEVTD EVIDGKNSIC FDEAENRLTS
    310 320 330
    IRGLLVYLMN DYEAKNPYDL IKQAEAKKEL EVFLDTQSI
    Length:339
    Mass (Da):38,343
    Last modified:June 1, 2003 - v1
    Checksum:i1459EE8AC906CF96
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE016830 Genomic DNA. Translation: AAO80551.1.
    RefSeqiNP_814481.1. NC_004668.1.
    WP_002355587.1. NZ_KE136527.1.

    Genome annotation databases

    EnsemblBacteriaiAAO80551; AAO80551; EF_0732.
    GeneIDi1199630.
    KEGGiefa:EF0732.
    PATRICi21851854. VBIEntFae7065_0677.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE016830 Genomic DNA. Translation: AAO80551.1.
    RefSeqiNP_814481.1. NC_004668.1.
    WP_002355587.1. NZ_KE136527.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3TXXX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L1-339[»]
    4A8HX-ray2.50A/B1-339[»]
    4A8PX-ray2.00A/B/C/D/E/F1-339[»]
    4A8TX-ray1.59A1-317[»]
    4AM8X-ray1.99A/B/C/D/E/F1-339[»]
    ProteinModelPortaliQ837U7.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi226185.EF0732.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAO80551; AAO80551; EF_0732.
    GeneIDi1199630.
    KEGGiefa:EF0732.
    PATRICi21851854. VBIEntFae7065_0677.

    Phylogenomic databases

    eggNOGiCOG0078.
    KOiK13252.
    OMAiMGMDFVQ.
    OrthoDBiEOG690MGV.

    Enzyme and pathway databases

    UniPathwayiUPA00534; UER00941.
    BioCyciEFAE226185:GHI1-718-MONOMER.
    BRENDAi2.1.3.3. 2095.
    2.1.3.6. 2095.
    SABIO-RKQ837U7.

    Family and domain databases

    Gene3Di3.40.50.1370. 2 hits.
    HAMAPiMF_02102. PTCase.
    InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    IPR002292. Orn/put_carbamltrans.
    IPR024903. PtcA.
    [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.
    TIGR04384. putr_carbamoyl. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700802 / V583.
    2. "The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction."
      Llacer J.L., Polo L.M., Tavarez S., Alarcon B., Hilario R., Rubio V.
      J. Bacteriol. 189:1254-1265(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-14, SUBUNIT, ENZYME REGULATION, CRYSTALLIZATION, KINETIC PARAMETERS.
      Strain: SD10.
    3. "Evolutionary relationships among bacterial carbamoyltransferases."
      Tricot C., De Coen J.-L., Momin P., Falmagne P., Stalon V.
      J. Gen. Microbiol. 135:2453-2464(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-30.
      Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
    4. "Fermentation of agmatine in Streptococcus faecalis: occurrence of putrescine transcarbamoylase."
      Roon R.J., Barker H.A.
      J. Bacteriol. 109:44-50(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
      Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
    5. "Structure and properties of the putrescine carbamoyltransferase of Streptococcus faecalis."
      Wargnies B., Lauwers N., Stalon V.
      Eur. J. Biochem. 101:143-152(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY, SUBUNIT, PH DEPENDENCE, ENZYME REGULATION.
    6. "The difficulty of annotating genes: the case of putrescine carbamoyltransferase."
      Naumoff D.G., Xu Y., Stalon V., Glansdorff N., Labedan B.
      Microbiology 150:3908-3911(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE NAME.

    Entry informationi

    Entry nameiPTC_ENTFA
    AccessioniPrimary (citable) accession number: Q837U7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: June 1, 2003
    Last modified: May 27, 2015
    This is version 92 of the entry and version 1 of the sequence. [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

    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

    External Data

    Dasty 3

    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 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.