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Q7P206 (CAPP_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate carboxylase
Short name=PEPC
Short name=PEPCase
EC=4.1.1.31
Gene names
Name:ppc
Ordered Locus Names:CV_0055
OrganismChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757) [Complete proteome] [HAMAP]
Taxonomic identifier243365 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium ›

Protein attributes

Sequence length898 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle By similarity. HAMAP-Rule MF_00595

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. HAMAP-Rule MF_00595

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00595

Sequence similarities

Belongs to the PEPCase type 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 898898Phosphoenolpyruvate carboxylase HAMAP-Rule MF_00595
PRO_0000166587

Sites

Active site1341 By similarity
Active site5641 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7P206 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 1F909AFD9E6C085E

FASTA89898,931
        10         20         30         40         50         60 
MSEHDKDLPL RADLACLDRL LSEVVGEQEG AVVSGAVQAI ALRRGDERSH PLPQLAPEAA 

        70         80         90        100        110        120 
ASLLRACGLY AQLFNIAEDL HHNRRRRAHQ LAGSAPQQGS LPRALQRLRQ DGVSFHALHQ 

       130        140        150        160        170        180 
LLSHAKVGAI LTAHPTEVQR QSVLDGHRAV RRFLSQLNAA DLTPEEREAL EAKLKRAILA 

       190        200        210        220        230        240 
LWQTSEIRHF KMTVRDEITN GVAYHPLAFF EALPALYRRL EREIGQLWGE EARLPSFIRV 

       250        260        270        280        290        300 
GSWIGGDRDG NPNVDAGLLR HAVTRQSQQA FEYYLQELKS LYRELSLSSR LVEAGAEVLA 

       310        320        330        340        350        360 
LAEQSPDQAV SRGEEPYRRA LATMQGKLRA TARLRGVELA CRWDERAPYR DHRELIQDLA 

       370        380        390        400        410        420 
SLSASLRAHG SALLADGRLS RLIRSVDVFG FFLMPLDLRQ HAAVHEGVVA ELFSAAGLEE 

       430        440        450        460        470        480 
YRALDEAARV RVLIRELATP RLLFSPYLRY GEQAEKELAI FREAAAIQRD FGVEAIGQCI 

       490        500        510        520        530        540 
ISNCASVSDI LALALLCKEA GLIRLEDGQP RASVNLVPLF ETIADLENSE AVMRALFALP 

       550        560        570        580        590        600 
WYKQLLDSRE RVQEVMLGYS DSNKDGGYLT SQWQLWQAET RLVKVFADAG ARLQLFHGRG 

       610        620        630        640        650        660 
GSVGRGGGPS YEAIVAQPAG SVAGRIRITE QGEVITAKYS DPAIAGRNLE ALVAATLEAS 

       670        680        690        700        710        720 
LGNIPGGEVD TALFDELSAS AFAAYRALVE TPGFMQYFLE ATPVTAIARL NIGSRPASRK 

       730        740        750        760        770        780 
SLSSIGDLRA IPWVFSWSQS RLMLPGWFGV GSAVAAYVQK HGDAGLAKLQ HLYRHSPFFQ 

       790        800        810        820        830        840 
VMLSNMEQVL AKADLGIARR FSELVADREL AARLFGAIEA EWRKTHDAFF AITGQAELLE 

       850        860        870        880        890 
GNPTLRRSLE TRLPFLDALG LLQADLLARL RAEPDDEDTL YAIHLTINGT SAGLRNTG

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References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016825 Genomic DNA. Translation: AAQ57735.1.
RefSeqNP_899725.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7P206.
ModBaseSearch...

Protein-protein interaction databases

STRING243365.CV_0055.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ57735; AAQ57735; CV_0055.
GeneID2551271.
KEGGcvi:CV_0055.
PATRIC21434876. VBIChrVio67196_0049.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2352.
HOGENOMHOG000238647.
KOK01595.
OMAAIPWVFG.
ProtClustDBPRK00009.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-55-MONOMER.

Family and domain databases

HAMAPMF_00595. PEPcase_type1.
InterProIPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamPF00311. PEPcase. 1 hit.
[Graphical view]
PRINTSPR00150. PEPCARBXLASE.
SUPFAMSSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAPP_CHRVO
AccessionPrimary (citable) accession number: Q7P206
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: December 15, 2003
Last modified: May 29, 2013
This is version 68 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

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