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

A4WJM7 (CAPPA_PYRAR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Phosphoenolpyruvate carboxylase

Short name=PEPC
Short name=PEPCase
EC=4.1.1.31
Gene names
Name:ppcA
Ordered Locus Names:Pars_1014
OrganismPyrobaculum arsenaticum (strain DSM 13514 / JCM 11321) [Complete proteome] [HAMAP]
Taxonomic identifier340102 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle By similarity. HAMAP-Rule MF_01904

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. HAMAP-Rule MF_01904

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01904

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01904

Sequence similarities

Belongs to the PEPCase type 2 family.

Ontologies

Keywords
   Biological processCarbon dioxide fixation
   LigandMagnesium
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcarbon fixation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

oxaloacetate metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tricarboxylic acid cycle

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phosphoenolpyruvate carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460Phosphoenolpyruvate carboxylase HAMAP-Rule MF_01904
PRO_0000309608

Sequences

Sequence LengthMass (Da)Tools
A4WJM7 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: BC72C5AC78BD73DC

FASTA46051,926
        10         20         30         40         50         60 
MMHIPRLMCT QHPDTTVKIT TAEEVDEAIV AYTAYGCDEV MVDYEGKMTP YGQPKEIVMK 

        70         80         90        100        110        120 
AIRGDVPLGD EFYITVRLPN PKLEEFDRAM LSLEAALVAN YFSRRYADAQ AVRWVVLPMV 

       130        140        150        160        170        180 
EDFDTVILVR RMLRRKAEIY KSETGVDVGE VEVIPLIEDA FVQVKAKVIV GEVFKSEEAR 

       190        200        210        220        230        240 
EVRVFLGKSD SAVRHGHLAS ALAIIYAMSK LKEFEAESGI RVRPILGMGS PPFRGALNNP 

       250        260        270        280        290        300 
RLAHLEVVQY AGYYTATIQS AVRYDTSLDE YVKVRESILN ACCGTRGLVG EEVLPLIQEA 

       310        320        330        340        350        360 
SAKYRSQAMK HVDKIAEVAR LVPSTRDRVS WKEYGRSLLD GDRVVHMPRA IVYTSAWYAM 

       370        380        390        400        410        420 
GFPPTLIDAP LLLELAKSDK LDAVFKLLPT YKMELEYDYE FFDPQTARNY LSEELVYAAV 

       430        440        450        460 
ELADYLGVEA RPTPTYTALL KMPRSEPNII ALSKYRKFLG 

« Hide

References

[1]"Complete sequence of Pyrobaculum arsenaticum DSM 13514."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13514 / JCM 11321.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000660 Genomic DNA. Translation: ABP50594.1.
RefSeqYP_001153246.1. NC_009376.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340102.Pars_1014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP50594; ABP50594; Pars_1014.
GeneID5054751.
KEGGpas:Pars_1014.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1892.
HOGENOMHOG000009826.
KOK01595.
OMADEYMPDY.

Enzyme and pathway databases

BioCycPARS340102:GHGQ-1027-MONOMER.

Family and domain databases

HAMAPMF_01904. PEPcase_type2.
InterProIPR007566. PEP_COase_arc-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamPF14010. PEPcase_2. 1 hit.
[Graphical view]
SUPFAMSSF51621. SSF51621. 1 hit.
TIGRFAMsTIGR02751. PEPCase_arch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCAPPA_PYRAR
AccessionPrimary (citable) accession number: A4WJM7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 44 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