CAPPA_SACS2
ID CAPPA_SACS2 Reviewed; 511 AA.
AC Q97WG4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_01904};
DE Short=PEPC {ECO:0000255|HAMAP-Rule:MF_01904};
DE Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_01904};
DE EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_01904};
GN Name=ppcA {ECO:0000255|HAMAP-Rule:MF_01904}; OrderedLocusNames=SSO2256;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=15516590; DOI=10.1128/jb.186.22.7754-7762.2004;
RA Ettema T.J., Makarova K.S., Jellema G.L., Gierman H.J., Koonin E.V.,
RA Huynen M.A., de Vos W.M., van der Oost J.;
RT "Identification and functional verification of archaeal-type
RT phosphoenolpyruvate carboxylase, a missing link in archaeal central
RT carbohydrate metabolism.";
RL J. Bacteriol. 186:7754-7762(2004).
CC -!- FUNCTION: Catalyzes the irreversible beta-carboxylation of
CC phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon
CC dicarboxylic acid source for the tricarboxylic acid cycle.
CC {ECO:0000255|HAMAP-Rule:MF_01904, ECO:0000269|PubMed:15516590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01904,
CC ECO:0000269|PubMed:15516590};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01904,
CC ECO:0000269|PubMed:15516590};
CC Note=Mg(2+) cannot be replaced by Mn(2+). {ECO:0000255|HAMAP-
CC Rule:MF_01904, ECO:0000269|PubMed:15516590};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by L-aspartate and L-
CC malate. PEPC activity is not affected by allosteric activators of
CC E.coli PEPC such as glucose 6-phosphate, fructose 1,6-bisphosphate, and
CC acetyl coenzyme A. {ECO:0000269|PubMed:15516590}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.09 mM for phosphoenolpyruvate {ECO:0000269|PubMed:15516590};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15516590};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius.
CC {ECO:0000269|PubMed:15516590};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01904}.
CC -!- SIMILARITY: Belongs to the PEPCase type 2 family. {ECO:0000255|HAMAP-
CC Rule:MF_01904}.
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DR EMBL; AE006641; AAK42423.1; -; Genomic_DNA.
DR PIR; H90395; H90395.
DR RefSeq; WP_009991534.1; NC_002754.1.
DR AlphaFoldDB; Q97WG4; -.
DR SMR; Q97WG4; -.
DR STRING; 273057.SSO2256; -.
DR EnsemblBacteria; AAK42423; AAK42423; SSO2256.
DR GeneID; 44127989; -.
DR KEGG; sso:SSO2256; -.
DR PATRIC; fig|273057.12.peg.2350; -.
DR eggNOG; arCOG04435; Archaea.
DR HOGENOM; CLU_517433_0_0_2; -.
DR InParanoid; Q97WG4; -.
DR OMA; QSAFRYD; -.
DR PhylomeDB; Q97WG4; -.
DR BRENDA; 4.1.1.31; 6163.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IDA:UniProtKB.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR HAMAP; MF_01904; PEPcase_type2; 1.
DR InterPro; IPR007566; PEP_COase_arc-type.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR Pfam; PF14010; PEPcase_2; 1.
DR PIRSF; PIRSF006677; UCP006677; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR02751; PEPCase_arch; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Carbon dioxide fixation; Lyase; Magnesium;
KW Reference proteome.
FT CHAIN 1..511
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000309615"
SQ SEQUENCE 511 AA; 58772 MW; 90E0795BB2EC2105 CRC64;
MRIIPRTMST QHPDNAKVPE WAKSEVIEGE DEVKEAFLAY SMYGVHEVMW DAEGKDVDTH
VVRKLLSNYP DYFREHILGK DLFLTYRLPN PKVEGADRKV FAETMESIPI TYDLAEKFYG
NGITIPVFEV ILPMTTSSLE IISVARYYEK AVANEDELEL YDGVKVKDLV GEIYPKVIEV
IPLVEDRDSL QNINNIVEGY YKVIKPKYMR VFLARSDPAM NYGMITAVLS VKIALSELYK
LSESLNFEIY PIIGVGSLPF RGHLSPENYE KVLEEYKGVY TYTIQSAFKY DYDYDKVKSA
ISSINNSRIS PARILEKYEE DVLRKITILY TERYQPIIES LANAINDVSV LLPRRRARKL
HIGLFGYSRS AGKVSLPRAI SFVGSLYSIG IPPELIGISS LSNLDEKEWD IFKQNYVNFK
HDLQTAARFL NWESFKLIKD IWKISEDTIA KIKEDIDYAE SVIGIKLGGI DYDSRKHILM
SSLFLLSFKE KILQESKKYL YEMALIRRSL G
