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Q8DW19 (PTC_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
Putrescine transcarbamoylase
Putrescine transcarbamylase
Gene names
Name:ptcA
Synonyms:aguB, arcB
Ordered Locus Names:SMU_262
OrganismStreptococcus mutans [Complete proteome] [HAMAP]
Taxonomic identifier1309 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

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 Probable. Is involved in the degradation pathway of the polyamine agmatine. Ref.1

Catalytic activity

Carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine. HAMAP MF_02102

Pathway

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

Subunit structure

Homotrimer By similarity. HAMAP MF_02102

Subcellular location

Cytoplasm By similarity HAMAP MF_02102.

Induction

Up-regulated by agmatine. Expressed under the control of carbohydrate catabolite repression. Ref.1

Sequence similarities

Belongs to the ATCase/OTCase family. PTCase subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Putrescine carbamoyltransferase HAMAP MF_02102
PRO_0000113034

Regions

Region54 – 585Carbamoyl phosphate binding By similarity
Region270 – 2734Putrescine binding By similarity

Sites

Binding site1051Carbamoyl phosphate By similarity
Binding site1321Carbamoyl phosphate By similarity
Site291Important for structural integrity By similarity
Site1451Important for structural integrity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DW19 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A51CA727DC5BA8CC

FASTA33938,519
        10         20         30         40         50         60 
MMKKTDYITT EDFSKEELLK LVDLSLKIKA CIKNGYYPPL LEHKSLGMIF QQTSTRTRVS 

        70         80         90        100        110        120 
FETAMSQLGG HAQYLAPGQI QLGGHETIED TSTVLSRLDD ILMARVERHQ SVVDLARCAS 

       130        140        150        160        170        180 
IPVINGMSDY NHPTQELGDL CTMIEHLPAG KKLEDCKVVF VGDATQVCFS LALITTKMGM 

       190        200        210        220        230        240 
EFVHFGPKGF QLNDMHKEKL DKICERSGGK YTVTDNEDAI EGADFLYTDV WYGLYEAELS 

       250        260        270        280        290        300 
EEERMQIFFP KYQVDSQMMA KAGADCKFMH CLPATRGEEI TDEVMDGPHS ICFDEAENRL 

       310        320        330 
TSIRGLLVYL LRDYREKNPY DLVKQEKAKE ELETFLKPE 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of an agmatine deiminase gene cluster in Streptococcus mutans UA159."
Griswold A.R., Chen Y.-Y.M., Burne R.A.
J. Bacteriol. 186:1902-1904(2004) [PubMed: 14996823] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN AGMATINE CATABOLISM, INDUCTION.
Strain: ATCC 700610 / UA159 / Serotype c.
[2]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed: 12397186] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159 / Serotype c.
[3]"Retrieving sequences of enzymes experimentally characterized but erroneously annotated: the case of the putrescine carbamoyltransferase."
Naumoff D.G., Xu Y., Glansdorff N., Labedan B.
BMC Genomics 5:52-52(2004) [PubMed: 15287962] [Abstract]
Cited for: REANNOTATION AS A PTCASE.
[4]"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: 15583144] [Abstract]
Cited for: GENE NAME.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BK004003 Genomic DNA. Translation: DAA04556.1.
AE014133 Genomic DNA. Translation: AAN58031.1.
RefSeqNP_720725.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ8DW19.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000014083; EBSTRP00000013565; EBSTRG00000014083.
GeneID1027850.
GenomeReviewsGene locus SMU_262 in contig AE014133_GR.
KEGGsmu:SMU_262.
NMPDRfig|210007.1.peg.238.
PATRIC19662785. VBIStrMut61772_0228.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000027080.
HOGENOMHBG579429.
OMALGMIFQQ.
ProtClustDBPRK02255.

Enzyme and pathway databases

BioCycSMUT210007:SMU_262-MONOMER.

Family and domain databases

HAMAPMF_02102. PTCase.
[Tree]
InterProIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR002292. Orn/put_carbamltrans.
IPR024903. PtcA.
[Graphical view]
KOK13252.
PfamPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSPR00100. AOTCASE.
PR00102. OTCASE.
SUPFAMSSF53671. Asp/Orn_carbamoyltranf. 1 hit.
TIGRFAMsTIGR00658. Orni_carb_tr. 1 hit.
PROSITEPS00097. CARBAMOYLTRANSFERASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTC_STRMU
AccessionPrimary (citable) accession number: Q8DW19
Secondary accession number(s): Q6IFZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families