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   27-MAR-2024, entry version 104.
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};
GN   OrderedLocusNames=SSO2256;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; 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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01904, 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   PaxDb; 273057-SSO2256; -.
DR   EnsemblBacteria; AAK42423; AAK42423; SSO2256.
DR   GeneID; 72910840; -.
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   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   NCBIfam; TIGR02751; PEPCase_arch; 1.
DR   Pfam; PF14010; PEPcase_2; 1.
DR   PIRSF; PIRSF006677; UCP006677; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 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
//