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A1RZN3 (CAPPA_THEPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:Tpen_1265
OrganismThermofilum pendens (strain Hrk 5) [Reference proteome] [HAMAP]
Taxonomic identifier368408 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermofilaceaeThermofilum

Protein attributes

Sequence length464 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
Reference 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 – 464464Phosphoenolpyruvate carboxylase HAMAP-Rule MF_01904
PRO_0000309617

Sequences

Sequence LengthMass (Da)Tools
A1RZN3 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 174AF466FC739834

FASTA46451,243
        10         20         30         40         50         60 
METPRLMCTQ HPDSTVKVPV QEEVEEAVRS FLVYGCDEVM SDYEGKLTPY AQPKEIVVKA 

        70         80         90        100        110        120 
GELGVPVGEG FYVTVRAPNP RLEDFDRVDL ALEAAVLANY YSYKRLGVQA VRWVVLPMTD 

       130        140        150        160        170        180 
SAETVRLVQR LLARKTRVLC EEVGQPCEQA QLVPLLEDVD SLLRVREILR DLHSALAELG 

       190        200        210        220        230        240 
SDPGVLRVFL GKSDSALKAG HIASALSLLY ALGESAKAGE ELGLEVKPIL GGGSPPFRGG 

       250        260        270        280        290        300 
VNNPRLVGVE VQRYRGYSTV TVQSAVRYDA SFSEYQEVRS KLLGGAGGEP GDAGGRVAEL 

       310        320        330        340        350        360 
ARLAASMYRS LASKYLDFVN EYARSVPTTR DRVSWREYGR ALELEDKLFS APRAIVYTAA 

       370        380        390        400        410        420 
WYSLGVPPTF LDADFVLEAY RGDFLDEVLG YLPGLEEEWR YDAQFYLPRL AGERLGEELV 

       430        440        450        460 
KKVDEALDAM GLRPEPLEPY EKLARTAPAE LRALLLGKVR GFLG 

« Hide

References

[1]"Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction."
Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E., Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M., Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B. expand/collapse author list , Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.
J. Bacteriol. 190:2957-2965(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hrk 5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000505 Genomic DNA. Translation: ABL78663.1.
RefSeqYP_920666.1. NC_008698.1.

3D structure databases

ProteinModelPortalA1RZN3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING368408.Tpen_1265.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL78663; ABL78663; Tpen_1265.
GeneID4600480.
KEGGtpe:Tpen_1265.

Phylogenomic databases

eggNOGCOG1892.
HOGENOMHOG000009826.
KOK01595.
OMADEYMPDY.

Enzyme and pathway databases

BioCycTPEN368408:GHSG-1320-MONOMER.

Family and domain databases

Gene3D3.20.20.60. 1 hit.
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_THEPD
AccessionPrimary (citable) accession number: A1RZN3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 49 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