ID   CAPPA_SULAC             Reviewed;         511 AA.
AC   Q4JCJ1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   24-JAN-2024, entry version 76.
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=Saci_0059;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   DOI=10.1111/j.1574-6968.1997.tb10477.x;
RA   Sako Y., Takai K., Nishizaka T., Ishida Y.;
RT   "Biochemical relationship of phosphoenolpyruvate carboxylases (PEPCs) from
RT   thermophilic archaea.";
RL   FEMS Microbiol. Lett. 153:159-165(1997).
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|Ref.2}.
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, ECO:0000269|Ref.2};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01904, ECO:0000269|Ref.2};
CC       Note=Mg(2+) cannot be replaced by Mn(2+). {ECO:0000255|HAMAP-
CC       Rule:MF_01904, ECO:0000269|Ref.2};
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|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.2 mM for phosphoenolpyruvate {ECO:0000269|Ref.2};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Optimum temperature is 90 degrees Celsius. Is extremely thermostable.
CC         No loss of activity is observed after incubation for 2 hours at 80
CC         degrees Celsius. The times required for 50% loss of activity are
CC         about 60 minutes at 90 degrees Celsius, 10 minutes at 95 degrees
CC         Celsius, and 1 minute at 100 degrees Celsius. {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01904,
CC       ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01904}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY79488.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000077; AAY79488.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015385346.1; NZ_CP046615.1.
DR   AlphaFoldDB; Q4JCJ1; -.
DR   SMR; Q4JCJ1; -.
DR   STRING; 330779.Saci_0059; -.
DR   GeneID; 78440414; -.
DR   KEGG; sai:Saci_0059; -.
DR   PATRIC; fig|330779.12.peg.55; -.
DR   eggNOG; arCOG04435; Archaea.
DR   HOGENOM; CLU_517433_0_0_2; -.
DR   Proteomes; UP000001018; 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_0000309614"
SQ   SEQUENCE   511 AA;  58355 MW;  1337C9AF4012A917 CRC64;
     MRKIPRTMST QHPDNAKVPE WNQGEAISGE NEIIEAYLAF SRYGVEEVMW DAEGKDVDTH
     VVRKLLSQYP EFFRHRILGK DIFLTYRVPN PKIEGAERKV FAETLNTIPI TYDLAEKFYG
     ENPNPPVFEV ILPFTTSYEE LIAVIKFYEK VIVNSDNTKL VDDTYVKDII GETNPKKIEV
     IPLIEDRDSM LRIDTIVGKY IEIERPPYLR VFLARSDPAM NYGLLSAVLS VKYALSRLSK
     MEKIYGVKIF PLLGVGSLPF RGHFSPYNVE NTLNEYRGIY TFTVQSAFKY DYEDDLVISA
     IKKVNGTNVT EKIELSEEDE EIISNVTRKY TQGYQNKIEA LADVINKVAL LLPRRRARKL
     HIGLFGYSRS TGKVTLPRAI SFVGSLYTIG IPPEIIGLSS LSKMTDQELN AIFNNYKYLK
     NDLQFAARFV NFEALQLLKD IWNIDAEVVK AIKEDIDYAE NSLGIRIGES DYMSKKHVLL
     STLALLSIKE GKLDEAKTYI KEMAIVRRAI G
//