ID   F9ZP62_ACICS            Unreviewed;       930 AA.
AC   F9ZP62;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Atc_1791 {ECO:0000313|EMBL:AEK58439.1};
OS   Acidithiobacillus caldus (strain SM-1).
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK58439.1, ECO:0000313|Proteomes:UP000006135};
RN   [1] {ECO:0000313|EMBL:AEK58439.1, ECO:0000313|Proteomes:UP000006135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM-1 {ECO:0000313|EMBL:AEK58439.1,
RC   ECO:0000313|Proteomes:UP000006135};
RX   PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA   You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA   Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT   "Unraveling the Acidithiobacillus caldus complete genome and its central
RT   metabolisms for carbon assimilation.";
RL   J. Genet. Genomics 38:243-252(2011).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|HAMAP-Rule:MF_00595}.
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:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP002573; AEK58439.1; -; Genomic_DNA.
DR   RefSeq; WP_004872419.1; NC_015850.1.
DR   AlphaFoldDB; F9ZP62; -.
DR   STRING; 990288.Atc_1791; -.
DR   GeneID; 69615318; -.
DR   KEGG; acu:Atc_1791; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 5287273at2; -.
DR   Proteomes; UP000006135; 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   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006135}.
FT   ACT_SITE        147
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        587
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   930 AA;  106485 MW;  FCC4B6B1DC3072E8 CRC64;
     MENKKVPNDR ALRARVKRLG NLLGEVLKEQ AGDRVFNAVE QLRQGYIRLH RREDPKLRKR
     LARFIDALPQ DDLVLVIRAF NTYFSLVNIA EEEFQHLQRR RLLQRSEALW VGSFEETFRA
     LQQQGIHSGQ LQYLLGQIRY LPVFTAHPTE SKRRTVLHGL RRIFLTSKML DDPSLSQEEE
     NDVLRQLKAQ IQILWETEEV RSNRPQVQDE VENGLFYFRD SLFNAVPMCY HAARRAVRRV
     YGNPNVDIPA FIRFGSWIGG DRDGNPNVTA AITGWALRTQ SMEVLREYQR RLADLYQLLG
     HSSRFCAVSP VLLASLERDA DDFPELAEWV NQRFPSEPYR RKLRYMMTRL DLRLRQLENG
     QILNEAAGPG YSSASEFLED LLLVRDSLRG HRDHYIAEHD VQNLVWLLET FGFHLAALDI
     RQESTVHGQT IAELFRDVAG FANYLEQPEE QRLLTLAEAL RRPGCLVTET PELSPLAAET
     CAMFRCIAQL RREVSPEAFG SYVISMTHEA SHILEVLLLA KEFGLAGWSR EGLYSEIAVT
     PLFETIHDLE RMEAVMSRLL DDPVYAEILR SQGNLQEVML GYSDSCKDGG ILSSSWSLYQ
     AQIRLAELAD RRRIQIRVFH GRGGSVGRGG GPTYEAIMAQ PPDTVRGQIK ITEQGEVLSF
     KYANLETAVY ELTVGVAGLI RASVGLVRRV ELDRPDYLQV MSELVEIGEA VYRDLTEHTP
     GFMDYFYEAT PLNEIAHMNI GSRPSHRHRG DRSMASIRAI PWVFAWAQSR HVLPAWYGLG
     SALARWRGDD PDRLNTLRDM AKHWPFFRAL LGNISMAMAK THLDLAREYA GLPQDQECAQ
     KIFAKIRAEY ELSLAELLTA LDLPAPLADN PTLAFSLQRR NVYMEPLNHI QLALLRRYRN
     EDTPQEFRET WLDPLLRTIN AIAAGQRNTG
//