ID   B9M086_GEODF            Unreviewed;       931 AA.
AC   B9M086;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 86.
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=Geob_2515 {ECO:0000313|EMBL:ACM20866.1};
OS   Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS   daltonii).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM20866.1, ECO:0000313|Proteomes:UP000007721};
RN   [1] {ECO:0000313|EMBL:ACM20866.1, ECO:0000313|Proteomes:UP000007721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC   {ECO:0000313|Proteomes:UP000007721};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kostka J., Richardson P.;
RT   "Complete sequence of Geobacter sp. FRC-32.";
RL   Submitted (JAN-2009) 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; CP001390; ACM20866.1; -; Genomic_DNA.
DR   RefSeq; WP_012647595.1; NC_011979.1.
DR   AlphaFoldDB; B9M086; -.
DR   STRING; 316067.Geob_2515; -.
DR   KEGG; geo:Geob_2515; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_7; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000007721; 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; 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; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 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:ACM20866.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007721}.
FT   ACT_SITE        180
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT   ACT_SITE        593
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   931 AA;  103841 MW;  A9C0E41850864BA9 CRC64;
     MAVMELFWQV EDQAARLAEL ISREGDLKEI PLRRDVRSLG MLLGMVIREQ AGEQAFIAEE
     ELRHLAIQHR QLHDNQATAC LDLPGERELQ EKAESIIGRM TVAEAYQIVK AFSTYFELTN
     LAETNHRKRR QRASRLISTA PDKPGSLRGT LLRMRQSGIS VEQALQWLRM VDVVPVFTAH
     PTDVARRVVH FKRRRIAQDL EALDTLPLTY AKALQGQNAM LAEVSALWQT DEVRRRKPTV
     LDEIKMGLDH YPDSLITPLP ALYEDMAAAI QEIYGLSISQ SELPTVVHFG SWIGGDRDGN
     PYVTADSTRA ALQKGREAIL GEYTTTLEEL RRLLTSSTCR VPVSPQLAAA VTNYHATLNF
     AELQKSAIPE CEQYRRFADC ILYRLRRTLR EPEHADAYVA AVEFSTDLHL IRASLAAGGG
     ERLARSLVDP LLRRIDTFGF HLHSLDIRQH AKVHATAVKE LAAGATTGTV TSAALPPAPS
     AATTELLDTL RAIAGLKRSY PPQAIQRYVI SGASCVQDSL ALVWLLELCG VRVAADNSGD
     PGLMPVPLFE SIEDLRQAPH ICRILWSSDD YKPYLDSWGR RQEVMLGYSD SNKDGGMLTS
     AWEIHKTHRE LHRVAAECGV RLVLFHGRGG TVGRGGGPTH RAIVAQPAGA FTGSLKITEQ
     GEVINWKYSD ASLAQRNLEV MVAASLEALA LTGMQEEQAS PKWAQTMETL SSDAFAFYRK
     HIAENPDIFP YFEQATPVLE FELAKIGSRP ARRGVTRDLS DLRAIPWGFG WMQSRHVIPG
     WFGVGYALER FAARQPGAMG QLQAMMGRFP FFIDLLRNVE LALTKVDLPL ARCYSTLVTD
     MELRQRVFDL VVEEYQRTRR MLLAITGQSH LLENNAPLAR SIRLRNPYVD PLSLIQIELL
     RRKRAGEESE ELNYVLAATI SGISAGLRNT G
//