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Q4JCJ1 (CAPPA_SULAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:Saci_0059
OrganismSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP]
Taxonomic identifier330779 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length511 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. Mg2+ can not be replaced by Mn2+. Ref.2

Enzyme regulation

Allosterically inhibited by L-aspartate and L-malate. PEPC activity is not affected by allosteric activators of E.coli PEPC such as glucose 6-phosphate, fructose 1,6-bisphosphate, and acetyl coenzyme A. Ref.2

Subunit structure

Homotetramer. Ref.2

Sequence similarities

Belongs to the PEPCase type 2 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.20 mM for phosphoenolpyruvate Ref.2

pH dependence:

Optimum pH is 8.0.

Temperature dependence:

Optimum temperature is 90 degrees Celsius. Is extremely thermostable. No loss of activity is observed after incubation for 2 hours at 80 degrees Celsius. The times required for 50% loss of activity are about 60 minutes at 90 degrees Celsius, 10 minutes at 95 degrees Celsius, and 1 minute at 100 degrees Celsius.

Sequence caution

The sequence AAY79488.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

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

Inferred from direct assay. Source: UniProtKB

oxaloacetate metabolic process

Inferred from direct assay. Source: UniProtKB

tricarboxylic acid cycle

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmagnesium ion binding

Inferred from direct assay. Source: UniProtKB

phosphoenolpyruvate carboxylase activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Phosphoenolpyruvate carboxylase HAMAP-Rule MF_01904
PRO_0000309614

Sequences

Sequence LengthMass (Da)Tools
Q4JCJ1 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 1337C9AF4012A917

FASTA51158,355
        10         20         30         40         50         60 
MRKIPRTMST QHPDNAKVPE WNQGEAISGE NEIIEAYLAF SRYGVEEVMW DAEGKDVDTH 

        70         80         90        100        110        120 
VVRKLLSQYP EFFRHRILGK DIFLTYRVPN PKIEGAERKV FAETLNTIPI TYDLAEKFYG 

       130        140        150        160        170        180 
ENPNPPVFEV ILPFTTSYEE LIAVIKFYEK VIVNSDNTKL VDDTYVKDII GETNPKKIEV 

       190        200        210        220        230        240 
IPLIEDRDSM LRIDTIVGKY IEIERPPYLR VFLARSDPAM NYGLLSAVLS VKYALSRLSK 

       250        260        270        280        290        300 
MEKIYGVKIF PLLGVGSLPF RGHFSPYNVE NTLNEYRGIY TFTVQSAFKY DYEDDLVISA 

       310        320        330        340        350        360 
IKKVNGTNVT EKIELSEEDE EIISNVTRKY TQGYQNKIEA LADVINKVAL LLPRRRARKL 

       370        380        390        400        410        420 
HIGLFGYSRS TGKVTLPRAI SFVGSLYTIG IPPEIIGLSS LSKMTDQELN AIFNNYKYLK 

       430        440        450        460        470        480 
NDLQFAARFV NFEALQLLKD IWNIDAEVVK AIKEDIDYAE NSLGIRIGES DYMSKKHVLL 

       490        500        510 
STLALLSIKE GKLDEAKTYI KEMAIVRRAI G 

« Hide

References

« Hide 'large scale' references
[1]"The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
J. Bacteriol. 187:4992-4999(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.
[2]"Biochemical relationship of phosphoenolpyruvate carboxylases (PEPCs) from thermophilic archaea."
Sako Y., Takai K., Nishizaka T., Ishida Y.
FEMS Microbiol. Lett. 153:159-165(1997)
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000077 Genomic DNA. Translation: AAY79488.1. Different initiation.
RefSeqYP_254781.1. NC_007181.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING330779.Saci_0059.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY79488; AAY79488; Saci_0059.
GeneID3472974.
KEGGsai:Saci_0059.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1892.
HOGENOMHOG000038601.
KOK01595.
ProtClustDBPRK13655.

Enzyme and pathway databases

BioCycSACI330779:GH9J-59-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]
PIRSFPIRSF006677. UCP006677. 1 hit.
SUPFAMSSF51621. SSF51621. 1 hit.
TIGRFAMsTIGR02751. PEPCase_arch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCAPPA_SULAC
AccessionPrimary (citable) accession number: Q4JCJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 45 of the entry and version 2 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