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

Q8XLE8 (CAPPA_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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:
Phosphoenolpyruvate carboxylase

Short name=PEPC
Short name=PEPCase
EC=4.1.1.31
Gene names
Name:ppcA
Ordered Locus Names:CPE1094
OrganismClostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195102 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length537 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.2

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. Ref.2

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01904

Subunit structure

Homodimer or homotetramer. Ref.2

Sequence similarities

Belongs to the PEPCase type 2 family.

Ontologies

Keywords
   Biological processCarbon dioxide fixation
   LigandMagnesium
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processcarbon fixation

Inferred from direct assay Ref.2. Source: UniProtKB

oxaloacetate metabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

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 direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 537537Phosphoenolpyruvate carboxylase HAMAP-Rule MF_01904
PRO_0000309593

Secondary structure

............................................................................... 537
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8XLE8 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: BCDD97C4E8EC8B8F

FASTA53760,494
        10         20         30         40         50         60 
MKIPCSMMTQ HPDNVETYIS IQQEPAEAIK GLTPQDKGGL GIEEVMIDFE GKLTPYHQTS 

        70         80         90        100        110        120 
QIALGLISNG IIPGKDVRVT PRIPNANKES VFRQLMSIMS IIETNVQSKE LTGTPAISEV 

       130        140        150        160        170        180 
VVPMIETGKE ISEFQDRVNS VVDMGNKNYK TKLDLNSVRI IPLVEDVPAL ANIDRILDEH 

       190        200        210        220        230        240 
YEIEKSKGHI LKDLRIMIAR SDTAMSYGLI SGVLSVLMAV DGAYKWGEKH GVTISPILGC 

       250        260        270        280        290        300 
GSLPFRGHFS EENIDEILAT YSGIKTFTFQ SALRYDHGEE ATKHAVRELK EKIAQSKPRN 

       310        320        330        340        350        360 
FSEEDKDLMK EFIGICSKHY LQTFLKVIDT VSFVSDFIPK NRDRLTKAKT GLEYNREVAN 

       370        380        390        400        410        420 
LDNVADLVKD EVLKQEILSI DNSKEYAVPR AISFTGAMYT LGMPPELMGM GRALNEIKTK 

       430        440        450        460        470        480 
YGQEGIDKLL EIYPILRKDL AFAARFANGG VSKKIIDEEA RQEYKEDMKY VNEILNLGLD 

       490        500        510        520        530 
YDFLNENEFY HTLLKTTKPI IMHLMGLEEN VMRNSTEELK ILNEWIVRMG KVRGSIG 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.
[2]"Expression, purification and crystallization of an archaeal-type phosphoenolpyruvate carboxylase."
Dharmarajan L., Kraszewski J.L., Mukhopadhyay B., Dunten P.W.
Acta Crystallogr. F 65:1193-1196(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, CRYSTALLIZATION.
Strain: 13 / Type A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000016 Genomic DNA. Translation: BAB80800.1.
RefSeqNP_562010.1. NC_003366.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ODMX-ray2.95A/B/C/D/E/F/G/H1-537[»]
ProteinModelPortalQ8XLE8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195102.CPE1094.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB80800; BAB80800; BAB80800.
GeneID989403.
KEGGcpe:CPE1094.
PATRIC19496138. VBICloPer59675_1166.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1892.
HOGENOMHOG000009826.
KOK01595.
OMADEYMPDY.
OrthoDBEOG6WDSG0.

Enzyme and pathway databases

BioCycCPER195102:GJFM-1138-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]
PIRSFPIRSF006677. UCP006677. 1 hit.
SUPFAMSSF51621. SSF51621. 1 hit.
TIGRFAMsTIGR02751. PEPCase_arch. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8XLE8.

Entry information

Entry nameCAPPA_CLOPE
AccessionPrimary (citable) accession number: Q8XLE8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 71 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references