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Q97WG4 (CAPPA_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:SSO2256
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]
Taxonomic identifier273057 [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 By similarity. HAMAP-Rule MF_01904

Sequence similarities

Belongs to the PEPCase type 2 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.09 mM for phosphoenolpyruvate Ref.2

pH dependence:

Optimum pH is 8.0.

Temperature dependence:

Optimum temperature is 85 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Phosphoenolpyruvate carboxylase HAMAP-Rule MF_01904
PRO_0000309615

Sequences

Sequence LengthMass (Da)Tools
Q97WG4 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 90E0795BB2EC2105

FASTA51158,772
        10         20         30         40         50         60 
MRIIPRTMST QHPDNAKVPE WAKSEVIEGE DEVKEAFLAY SMYGVHEVMW DAEGKDVDTH 

        70         80         90        100        110        120 
VVRKLLSNYP DYFREHILGK DLFLTYRLPN PKVEGADRKV FAETMESIPI TYDLAEKFYG 

       130        140        150        160        170        180 
NGITIPVFEV ILPMTTSSLE IISVARYYEK AVANEDELEL YDGVKVKDLV GEIYPKVIEV 

       190        200        210        220        230        240 
IPLVEDRDSL QNINNIVEGY YKVIKPKYMR VFLARSDPAM NYGMITAVLS VKIALSELYK 

       250        260        270        280        290        300 
LSESLNFEIY PIIGVGSLPF RGHLSPENYE KVLEEYKGVY TYTIQSAFKY DYDYDKVKSA 

       310        320        330        340        350        360 
ISSINNSRIS PARILEKYEE DVLRKITILY TERYQPIIES LANAINDVSV LLPRRRARKL 

       370        380        390        400        410        420 
HIGLFGYSRS AGKVSLPRAI SFVGSLYSIG IPPELIGISS LSNLDEKEWD IFKQNYVNFK 

       430        440        450        460        470        480 
HDLQTAARFL NWESFKLIKD IWKISEDTIA KIKEDIDYAE SVIGIKLGGI DYDSRKHILM 

       490        500        510 
SSLFLLSFKE KILQESKKYL YEMALIRRSL G 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[2]"Identification and functional verification of archaeal-type phosphoenolpyruvate carboxylase, a missing link in archaeal central carbohydrate metabolism."
Ettema T.J., Makarova K.S., Jellema G.L., Gierman H.J., Koonin E.V., Huynen M.A., de Vos W.M., van der Oost J.
J. Bacteriol. 186:7754-7762(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006641 Genomic DNA. Translation: AAK42423.1.
PIRH90395.
RefSeqNP_343633.1. NC_002754.1.

3D structure databases

ProteinModelPortalQ97WG4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273057.SSO2256.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK42423; AAK42423; SSO2256.
GeneID1453750.
KEGGsso:SSO2256.

Phylogenomic databases

eggNOGCOG1892.
HOGENOMHOG000038601.
KOK01595.
OMADEYMPDY.

Enzyme and pathway databases

BioCycSSOL273057:GCH2-2108-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_SULSO
AccessionPrimary (citable) accession number: Q97WG4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 63 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