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Q97WG4

- CAPPA_SULSO

UniProt

Q97WG4 - CAPPA_SULSO

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Protein
Phosphoenolpyruvate carboxylase
Gene
ppcA, SSO2256
Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.1 Publication

Catalytic activityi

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.1 Publication

Cofactori

Magnesium. Mg2+ can not be replaced by Mn2+.1 Publication

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=0.09 mM for phosphoenolpyruvate1 Publication

pH dependencei

Optimum pH is 8.0.

Temperature dependencei

Optimum temperature is 85 degrees Celsius.

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB
  2. phosphoenolpyruvate carboxylase activity Source: UniProtKB

GO - Biological processi

  1. carbon fixation Source: UniProtKB
  2. oxaloacetate metabolic process Source: UniProtKB
  3. tricarboxylic acid cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbon dioxide fixation

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-2108-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxylase (EC:4.1.1.31)
Short name:
PEPC
Short name:
PEPCase
Gene namesi
Name:ppcA
Ordered Locus Names:SSO2256
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 511511Phosphoenolpyruvate carboxylaseUniRule annotation
PRO_0000309615Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi273057.SSO2256.

Structurei

3D structure databases

ProteinModelPortaliQ97WG4.

Family & Domainsi

Sequence similaritiesi

Belongs to the PEPCase type 2 family.

Phylogenomic databases

eggNOGiCOG1892.
HOGENOMiHOG000038601.
KOiK01595.
OMAiDEYMPDY.

Family and domain databases

HAMAPiMF_01904. PEPcase_type2.
InterProiIPR007566. PEP_COase_arc-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF14010. PEPcase_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006677. UCP006677. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR02751. PEPCase_arch. 1 hit.

Sequencei

Sequence statusi: Complete.

Q97WG4-1 [UniParc]FASTAAdd to Basket

« Hide

MRIIPRTMST QHPDNAKVPE WAKSEVIEGE DEVKEAFLAY SMYGVHEVMW    50
DAEGKDVDTH VVRKLLSNYP DYFREHILGK DLFLTYRLPN PKVEGADRKV 100
FAETMESIPI TYDLAEKFYG NGITIPVFEV ILPMTTSSLE IISVARYYEK 150
AVANEDELEL YDGVKVKDLV GEIYPKVIEV IPLVEDRDSL QNINNIVEGY 200
YKVIKPKYMR VFLARSDPAM NYGMITAVLS VKIALSELYK LSESLNFEIY 250
PIIGVGSLPF RGHLSPENYE KVLEEYKGVY TYTIQSAFKY DYDYDKVKSA 300
ISSINNSRIS PARILEKYEE DVLRKITILY TERYQPIIES LANAINDVSV 350
LLPRRRARKL HIGLFGYSRS AGKVSLPRAI SFVGSLYSIG IPPELIGISS 400
LSNLDEKEWD IFKQNYVNFK HDLQTAARFL NWESFKLIKD IWKISEDTIA 450
KIKEDIDYAE SVIGIKLGGI DYDSRKHILM SSLFLLSFKE KILQESKKYL 500
YEMALIRRSL G 511
Length:511
Mass (Da):58,772
Last modified:October 1, 2001 - v1
Checksum:i90E0795BB2EC2105
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006641 Genomic DNA. Translation: AAK42423.1.
PIRiH90395.
RefSeqiNP_343633.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK42423; AAK42423; SSO2256.
GeneIDi1453750.
KEGGisso:SSO2256.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006641 Genomic DNA. Translation: AAK42423.1 .
PIRi H90395.
RefSeqi NP_343633.1. NC_002754.1.

3D structure databases

ProteinModelPortali Q97WG4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273057.SSO2256.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK42423 ; AAK42423 ; SSO2256 .
GeneIDi 1453750.
KEGGi sso:SSO2256.

Phylogenomic databases

eggNOGi COG1892.
HOGENOMi HOG000038601.
KOi K01595.
OMAi DEYMPDY.

Enzyme and pathway databases

BioCyci SSOL273057:GCH2-2108-MONOMER.

Family and domain databases

HAMAPi MF_01904. PEPcase_type2.
InterProi IPR007566. PEP_COase_arc-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view ]
Pfami PF14010. PEPcase_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF006677. UCP006677. 1 hit.
SUPFAMi SSF51621. SSF51621. 1 hit.
TIGRFAMsi TIGR02751. PEPCase_arch. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiCAPPA_SULSO
AccessioniPrimary (citable) accession number: Q97WG4
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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