ID   D5H4R6_SALRM            Unreviewed;       928 AA.
AC   D5H4R6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
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   ECO:0000313|EMBL:CBH23021.1};
GN   OrderedLocusNames=SRM_00100 {ECO:0000313|EMBL:CBH23021.1};
OS   Salinibacter ruber (strain M8).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=761659 {ECO:0000313|EMBL:CBH23021.1, ECO:0000313|Proteomes:UP000000933};
RN   [1] {ECO:0000313|EMBL:CBH23021.1, ECO:0000313|Proteomes:UP000000933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8 {ECO:0000313|EMBL:CBH23021.1,
RC   ECO:0000313|Proteomes:UP000000933};
RX   PubMed=20164864; DOI=10.1038/ismej.2010.6;
RA   Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA   Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA   Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA   Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT   "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT   in two coexisting Salinibacter ruber strains.";
RL   ISME J. 4:882-895(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8 {ECO:0000313|Proteomes:UP000000933};
RG   Genoscope;
RT   "Genome sequence of Salinibacter ruber M8.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; FP565814; CBH23021.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5H4R6; -.
DR   KEGG; srm:SRM_00100; -.
DR   PATRIC; fig|761659.10.peg.113; -.
DR   HOGENOM; CLU_006557_2_0_10; -.
DR   Proteomes; UP000000933; 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}.
FT   REGION          82..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        578
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   928 AA;  103680 MW;  8E42493D0833BFCA CRC64;
     MLGHIAEEQS GEALFEHVEG LRALCKAAEQ EDAPEKREEA AERIAALDQD TLERLLHVYT
     TFFHLVNQAE QQEIIRINRE RARQSGPSEW PLGPGDGPGA DGAEPRPQSI DAAVADLKAE
     GYTADEVVAF FRQLDIQPTL TAHPTEARRR SVLRKEQHIA DLLSTLRRPD ATPDERAETL
     DRLYSQVAFL LGTDEVRAER PTVREEVEQG HYFLHGSIWD TIPAIHRDVQ QALRRHYDAT
     AELPAFLQYR SWIGSDRDGN PNVTADVTRW TVARQRRTTL EHYLDEIDEL RDDLSISTRQ
     LTVSDALEAS LEADAEEIAL PDDVRRQYQR EPYRLKLCYI EERLRGLLDR IDATDVAAMA
     GAYTADDLLA DLDLIAESLQ GHGFEDAAQS GQLHRLRSLV KTFGFHLAAL DVRQHSGVHE
     DTVAALLDAG DVVDDYGALS EEEKLEVLSR ELQNPRPLVS RHADLPADAA ELMEVFGVLR
     AMHAVDPDIV GSYVVSMTHT VSDLLEPMLL AKEAGLGAVV DGSYRCPLDV VPLFETIEDL
     DAADDRMKTL FTHPVYAAQL EGRDGFQEIM LGYSDSNKDG GYWMANWALH KAIHALGVVC
     DEHDVDLRLF HGRGGTVGRG GGHTSQAIRA LPPVVHNGRI RMTEQGEIIS FRYALPDIAR
     RHVEQIVNAT LTATARAQNT PAPENPLLAD KVSMESDVVA LMDRLAEEGM SAYRAFIDDP
     EGWQWYTAAT PIEHISRLPI ASRPVSRASA GEQVEFENLR AIPWVFAWTQ TRYIAPGWYG
     TGQGLATLLE DEPDARDTLR DLYENWPFFR TVLDSAQREM ARARLPIAER YDALAEVETS
     FHAPIVDDYE RAESAILEIT DQAALFDGNP VLKKSIELRN PYTDVLNLIQ IELLKRYRAS
     TDDAEQETLR EAIFLSINGV AAAMQSTG
//