Q4JCJ1 (CAPPA_SULAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoenolpyruvate carboxylase
Short name=PEPC
Short name=PEPCase
EC=4.1.1.31

Gene names

Name:	ppcA
Ordered Locus Names:	Saci_0059

Organism

Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP]

Taxonomic identifier

330779 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus › Sulfolobus acidocaldarius

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Carbon dioxide fixation
Ligand	Magnesium
Molecular function	Lyase
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological_process	carbon 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_function	magnesium ion binding Inferred from direct assay. Source: UniProtKB phosphoenolpyruvate carboxylase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 511	511	Phosphoenolpyruvate carboxylase HAMAP-Rule MF_01904		PRO_0000309614

Sequences

	Sequence		Length	Mass (Da)
	Q4JCJ1 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 1337C9AF4012A917	FASTA	511	58,355
	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

References

	« Hide 'large scale' referencesShow '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.
RefSeq	YP_254781.1. NC_007181.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	330779.Saci_0059.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAY79488; AAY79488; Saci_0059.
GeneID	3472974.
KEGG	sai:Saci_0059.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1892.
HOGENOM	HOG000038601.
KO	K01595.
ProtClustDB	PRK13655.
Enzyme and pathway databases
BioCyc	SACI330779:GH9J-145-MONOMER.
Family and domain databases
HAMAP	MF_01904. PEPcase_type2.
InterPro	IPR007566. PEP_COase_arc-type. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view]
PIRSF	PIRSF006677. UCP006677. 1 hit.
SUPFAM	SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR02751. PEPCase_arch. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CAPPA_SULAC

Accession

Primary (citable) accession number: Q4JCJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	November 13, 2007
Last modified:	May 1, 2013
This is version 42 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program