Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C1D1N4 (C1D1N4_DEIDV) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 37. Feed History...

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

Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate carboxylase HAMAP-Rule MF_00595

Short name=PEPC HAMAP-Rule MF_00595
Short name=PEPCase HAMAP-Rule MF_00595
EC=4.1.1.31 HAMAP-Rule MF_00595
Gene names
Name:ppc HAMAP-Rule MF_00595
Ordered Locus Names:Deide_08820 EMBL ACO45758.1
OrganismDeinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP] EMBL ACO45758.1
Taxonomic identifier546414 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length828 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 SAAS SAAS021135

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. HAMAP-Rule MF_00595 SAAS SAAS018129

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00595 SAAS SAAS018129

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00595

Sequence similarities

Belongs to the PEPCase type 1 family. HAMAP-Rule MF_00595

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1311 By similarity HAMAP-Rule MF_00595
Active site5041 By similarity HAMAP-Rule MF_00595

Sequences

Sequence LengthMass (Da)Tools
C1D1N4 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 9303FC0860DD8325

FASTA82891,506
        10         20         30         40         50         60 
MGIRSDVNLL GRTLGQVLKE QEGEAFFELV ERTRALVREV RAGGDDTELS AMLAELSGAE 

        70         80         90        100        110        120 
AGRLARAFTW YFQLVNLAEE YERVRVLSSV EGVRPQSLEQ ALMDLKAQGM SAQEVEALLS 

       130        140        150        160        170        180 
RLDLGLTFTA HPTEMRRRTV RGHLVEVARA IPELSQPTLA EDATERIAAH VEAMWSTPEL 

       190        200        210        220        230        240 
RRLKPTVLDE VKGGLSYMPN IARALPMLQR DLSRAFERVY GHSSEAQLPL SFTSWMGGDR 

       250        260        270        280        290        300 
DGNPFVTPQA THDALALHRE RAREVLISSI AQAYADLSQE KEGQEPYRQE LRALHNAVRD 

       310        320        330        340        350        360 
GEPVELLPRL EALHRRLCAE GQRRSADQLL TPLLTVARVF GQHLVSLDIR EHSAQTGAAV 

       370        380        390        400        410        420 
AALLKAAGVE NDYEALAEHA RQEVLTRELR SRRPLWPAGE PFPETLETAI GPIRQVQAAT 

       430        440        450        460        470        480 
RQVGPRAFGR YIVSMAESVS DVLEPLILAR EVGFRALPVP LFETLDDLQR APQVVWELLS 

       490        500        510        520        530        540 
IPEYRAALGS DVQEIMLGYS DSNKDAGFLA ANWALHEAQR AISEVCRRAG VRWRFFHGRG 

       550        560        570        580        590        600 
TSIGRGGGPA SRAILGQPAG TIDAGLRITE QGEALADKYS HPVLARRNLE QALYGVLLAA 

       610        620        630        640        650        660 
ARPAVAPPEA WTRGMDTAAR ASAAAYRALV DDPGFLPFFE AVTPIHEIAR LNIASRPVRR 

       670        680        690        700        710        720 
PGAPTLGNLR AIPWVMCWTQ NRANLPGWYG LHEGLSTLGV DLAREMYRDW PFFRTVLDNA 

       730        740        750        760        770        780 
QMSLAKSDPL IFDEYLRLMG EHPLATQLKA AYQATVALVQ DVVGAPLMAG EPRLKESIAL 

       790        800        810        820 
RNPYIDPIHR IQVELLRRSR SKEGGLDEFE VPLLLSIQGI AAGVRNTG 

« Hide

References

[1]"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti."
de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.
PLoS Genet. 5:E1000434-E1000434(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001114 Genomic DNA. Translation: ACO45758.1.
RefSeqYP_002785512.1. NC_012526.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING546414.Deide_08820.

Proteomic databases

PaxDbC1D1N4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO45758; ACO45758; Deide_08820.
GeneID7739110.
KEGGddr:Deide_08820.
PATRIC21615446. VBIDeiDes121019_1007.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2352.
HOGENOMHOG000238647.
KOK01595.
OMAPLIEREY.
OrthoDBEOG6TJ7T8.

Enzyme and pathway databases

BioCycDDES546414:GHOM-1005-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. 2 hits.
[Graphical view]
PRINTSPR00150. PEPCARBXLASE.
SUPFAMSSF51621. SSF51621. 1 hit.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC1D1N4_DEIDV
AccessionPrimary (citable) accession number: C1D1N4
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: June 11, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)