ID   D0MJ89_RHOM4            Unreviewed;       938 AA.
AC   D0MJ89;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=Rmar_1661 {ECO:0000313|EMBL:ACY48547.1};
OS   Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS   obamensis).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC   Rhodothermus.
OX   NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY48547.1, ECO:0000313|Proteomes:UP000002221};
RN   [1] {ECO:0000313|EMBL:ACY48547.1, ECO:0000313|Proteomes:UP000002221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43812 / DSM 4252 / R-10
RC   {ECO:0000313|Proteomes:UP000002221};
RX   PubMed=21304669; DOI=10.4056/sigs.46736;
RA   Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA   Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Detter J.C.;
RT   "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL   Stand. Genomic Sci. 1:283-291(2009).
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; CP001807; ACY48547.1; -; Genomic_DNA.
DR   RefSeq; WP_012844158.1; NC_013501.1.
DR   AlphaFoldDB; D0MJ89; -.
DR   STRING; 518766.Rmar_1661; -.
DR   KEGG; rmr:Rmar_1661; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_10; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002221; 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   Pyruvate {ECO:0000313|EMBL:ACY48547.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002221}.
FT   ACT_SITE        157
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        597
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   938 AA;  108217 MW;  548CA56FE86208FF CRC64;
     MSVLPPLQIE IEGTGISRPL SEHVNLLGGL LGQVIQEMAG PEMLELVETL RRLCKQAAQE
     NRPELREQAY TRIHSATYDE LLWLLRAYTA FFHLVNQAEQ QEIIRINRER AQQSTPEHPR
     PESIDEAILA LKQQGRTLDD VLALLERLDI QPTLTAHPTE ARRRSILYKQ QHIARLLSQQ
     RRCRLTPEEQ EALLVDLHNQ ITLLLGTAEV REERPTVRDE VEQGLYFIQS TIWEAVPRIH
     EDVRRALRRY YGTDADFRPF LRYRSWIGSD RDGNPYVTPE ITRWTALTQR RLVLQRYMEE
     LRQLRRRLSL SDRYVPPPEE LRRSLARDAR EVSLPPHVLR QFRHESFRLK ISYIMGRLHG
     LLQALDDPTQ PAPDYDADAF VEDLRLLQRC LEACGLERIA RHDQLSRLLV LVQTFGFHLV
     TLDVRQHSSV HEAAVAELLR LAGVENDYRA LPESRRQELL AEELSNPRPL LPPGARVSEA
     TRQVLETFAA IRELVQLDPR LVGSYIVSMT HTVSDLLEPM LLAKEVGLWH YERDPRTGKP
     GHVRCPIDFV PLFETIEDLE AAASRMEAIL SHPVYRMQVA ARGGFQEIML GYSDSTKDGG
     YWMANWALHR AQEQLAEVCL RHGVDFRLFH GRGGTVGRGG GRANQAILAM PPVVHNGRIR
     FTEQGEVISF RYALPEIAHR HLEQIVNAML RVVGLPAASG TDGTDPATRN RLMDELATRS
     MRAYRRLIDA PDFWSWYTRI TPIDQISRLP IASRPVSRSS AREVDFESLR AIPWVFAWTQ
     VRYLIPGWFG IGQALDELLQ TSPEHLETLR TWYRSWPFFR TVLQNAQREM VRARLEIAAY
     YDRLLGDGPT AFHQMIEEDY HRARTAILRI TDQEELLDHD PIIRKSVQLR NPYTDVLNLV
     QLELMRRYRQ APEADREPLR RALFLSINGI AAAMQSTG
//