ID   CAPPA_SULIM             Reviewed;         511 AA.
AC   C3MTS7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
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=M1425_0069;
OS   Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=427317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.14.25 / Kamchatka #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01904};
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; CP001400; ACP36961.1; -; Genomic_DNA.
DR   RefSeq; WP_012710248.1; NC_012588.1.
DR   AlphaFoldDB; C3MTS7; -.
DR   SMR; C3MTS7; -.
DR   GeneID; 84060555; -.
DR   KEGG; sia:M1425_0069; -.
DR   HOGENOM; CLU_517433_0_0_2; -.
DR   Proteomes; UP000001350; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium.
FT   CHAIN           1..511
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000216174"
SQ   SEQUENCE   511 AA;  58806 MW;  63438D39932AF2D5 CRC64;
     MRIIPRTMST QHPDNAKVPE WAKSEVIEGE DEVKEAFLAY SMYGVHEVMW DAEGKDVDTH
     VVRKLLSNYP DYFREHILGK DVFLTYRLPN PKVEGADRKV FAETMESIPI TYDLAEKFYG
     NGITVPVFEV ILPMTTSNLE IISVARYYEK AVANEDELEL YNGVKVKDLV GEIYPKVIEV
     IPLVEDRDSL QNIDNIVEGY YKVIKPKYMR VFLARSDPAM NYGMITAVLS VKIALSELYK
     LSESLNFEIY PIIGVGSLPF RGHLSPENYE KVLEEYKGVY TYTIQSAFKY DYDYDKVKSA
     ISSINNSRIG PAKILEKYEE DVLRKITILY TERYQPIIES LANAINDVSV LLPRRRARKL
     HIGLFGYSRS AGKVSLPRAI SFVGSLYSIG IPPELIGISS LSNLDEKEWD IFKQNYVNFK
     HDLQTAARFF NWESFELIKD IWKISEDTIA KIKEDIDYAE SVIGIKLGDI DYDSRKHILM
     SSLFLLSFKE KILQESKKYL YEMALIRRSL G
//