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Q837U7 (PTC_ENTFA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putrescine carbamoyltransferase

Short name=PTC
Short name=PTCase
EC=2.1.3.6
Alternative name(s):
Agmatine catabolism protein B
Putrescine transcarbamoylase
Putrescine transcarbamylase
Gene names
Name:ptcA
Synonyms:agcB, argF-2
Ordered Locus Names:EF_0732
OrganismEnterococcus faecalis (strain ATCC 700802 / V583) [Reference proteome] [HAMAP]
Taxonomic identifier226185 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Catalytic activity

Carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine. Ref.4

Enzyme regulation

Inhibited by spermidine and N-(phosphonoacetyl)-putrescine. Ref.2 Ref.5

Pathway

Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from N-carbamoylputrescine (transferase route): step 1/1. HAMAP-Rule MF_02102

Subunit structure

Homotrimer. Ref.2 Ref.5

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02102.

Sequence similarities

Belongs to the ATCase/OTCase family. PTCase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=58 µM for carbamoyl phosphate Ref.2

KM=2.3 mM for putrescine

pH dependence:

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.

Ontologies

Keywords
   Biological processPolyamine biosynthesis
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processputrescine biosynthetic process from arginine via N-carbamoylputrescine

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionamino acid binding

Inferred from electronic annotation. Source: InterPro

putrescine carbamoyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Putrescine carbamoyltransferase HAMAP-Rule MF_02102
PRO_0000112923

Regions

Region52 – 565Carbamoyl phosphate binding By similarity
Region268 – 2714Putrescine binding By similarity

Sites

Binding site1031Carbamoyl phosphate By similarity
Binding site1301Carbamoyl phosphate By similarity
Site271Important for structural integrity By similarity
Site1431Important for structural integrity By similarity

Secondary structure

.............................................................. 339
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q837U7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 1459EE8AC906CF96

FASTA33938,343
        10         20         30         40         50         60 
MKRDYVTTET YTKEEMHYLV DLSLKIKEAI KNGYYPQLLK NKSLGMIFQQ SSTRTRVSFE 

        70         80         90        100        110        120 
TAMEQLGGHG EYLAPGQIQL GGHETIEDTS RVLSRLVDIL MARVERHHSI VDLANCATIP 

       130        140        150        160        170        180 
VINGMSDYNH PTQELGDLCT MVEHLPEGKK LEDCKVVFVG DATQVCFSLG LITTKMGMNF 

       190        200        210        220        230        240 
VHFGPEGFQL NEEHQAKLAK NCEVSGGSFL VTDDASSVEG ADFLYTDVWY GLYEAELSEE 

       250        260        270        280        290        300 
ERMKVFYPKY QVNQEMMDRA GANCKFMHCL PATRGEEVTD EVIDGKNSIC FDEAENRLTS 

       310        320        330 
IRGLLVYLMN DYEAKNPYDL IKQAEAKKEL EVFLDTQSI 

« Hide

References

« Hide 'large scale' references
[1]"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis."
Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A. expand/collapse author list , Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.
Science 299:2071-2074(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016830 Genomic DNA. Translation: AAO80551.1.
RefSeqNP_814481.1. NC_004668.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ837U7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226185.EF0732.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO80551; AAO80551; EF_0732.
GeneID1199630.
KEGGefa:EF0732.
PATRIC21851854. VBIEntFae7065_0677.

Phylogenomic databases

eggNOGCOG0078.
KOK13252.
OMAIFYPKYQ.
OrthoDBEOG690MGV.
ProtClustDBPRK02255.

Enzyme and pathway databases

BioCycEFAE226185:GHI1-718-MONOMER.
SABIO-RKQ837U7.
UniPathwayUPA00534; UER00941.

Family and domain databases

Gene3D3.40.50.1370. 2 hits.
HAMAPMF_02102. PTCase.
InterProIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR002292. Orn/put_carbamltrans.
IPR024903. PtcA.
[Graphical view]
PfamPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSPR00100. AOTCASE.
PR00102. OTCASE.
SUPFAMSSF53671. SSF53671. 1 hit.
TIGRFAMsTIGR00658. orni_carb_tr. 1 hit.
ProtoNetSearch...

Entry information

Entry namePTC_ENTFA
AccessionPrimary (citable) accession number: Q837U7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways