ID   Q2S6D5_SALRD            Unreviewed;       957 AA.
AC   Q2S6D5;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 112.
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:ABC43864.1};
GN   OrderedLocusNames=SRU_0093 {ECO:0000313|EMBL:ABC43864.1};
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC43864.1, ECO:0000313|Proteomes:UP000008674};
RN   [1] {ECO:0000313|EMBL:ABC43864.1, ECO:0000313|Proteomes:UP000008674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31
RC   {ECO:0000313|Proteomes:UP000008674};
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC43864.1; -; Genomic_DNA.
DR   RefSeq; WP_011402879.1; NC_007677.1.
DR   RefSeq; YP_444246.1; NC_007677.1.
DR   AlphaFoldDB; Q2S6D5; -.
DR   STRING; 309807.SRU_0093; -.
DR   EnsemblBacteria; ABC43864; ABC43864; SRU_0093.
DR   KEGG; sru:SRU_0093; -.
DR   PATRIC; fig|309807.25.peg.102; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_10; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008674; 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:UP000008674}.
FT   REGION          111..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        607
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   957 AA;  107032 MW;  09EDFEE3C6EE3C4E CRC64;
     MPRWDDLDLE TEGTGISKPL SRQVNLVGSM LGHIAEEQSG EALFEHVEGL RALCKAAEQE
     DAPEKREEAA ERIAALDQDT LERLLHVYTT FFHLVNQAEQ QEIIRINRER ARQSGPSEWP
     LGPGDGPGAD GAEPRPQSID AAVADLKAEG YTADEVVAFF RQLDIQPTLT AHPTEARRRS
     VLRKEQHIAD LLSTLRRPDA TPDERAETLD RLYSQVAFLL GTDEVRAERP TVREEVEQGH
     YFLHGSIWDT IPAIHRDVQQ ALRRHYDATA ELPAFLQYRS WIGSDRDGNP NVTADVTRWT
     VARQRRTTLE HYLDEIDELR DDLSISTRQL TVSDALEASL EADAEEIALP DDVRRQYQRE
     PYRLKLCYIE ERLRGLLDRI DATDVAAMAG AYAADDLLAD LDLIAESLQG HGFEDAAQSG
     QLHRLRSLVK TFGFHLAALD VRQHSRVHED TVAALLDAGD VVDDYGALSE EEKLEVLSRE
     LQNPRPLVSR HADLPADAAE LMEVFGVLRA MHAVDPDIVG SYVVSMTHTV SDLLEPMLLA
     KEAGLGAVVD GSYRCPLDVV PLFETIEDLD AADDRMETLF THPVYAAQLE GRDGFQEIML
     GYSDSNKDGG YWMANWALHK AIHALGVVCD EHDVDLRLFH GRGGTVGRGG GHTSQAIRAL
     PPVVHNGRIR MTEQGEIISF RYALPDIARR HVEQIVNATL TATARAQNTP APENPLLADK
     VSMESDVVAL MDRLAEEGMS AYREFIDDPE GWQWYTAATP IEHISRLPIA SRPVSRASEG
     EQVEFENLRA IPWVFAWTQT RYIAPGWYGT GQGLATLLEN EPDARDTLRD LYENWPFFRT
     VLDSAQREMA RARLPIAERY DALAEVETSF HAPIVDDYER AESAILEITD QAALFDGNPV
     LKKSIELRNP YTDVLNLIQI ELLKRYRAST DDAEQEALRE AIFLSINGVA AAMQSTG
//