ID   E8WXD5_GRATM            Unreviewed;       931 AA.
AC   E8WXD5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
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=AciX9_0396 {ECO:0000313|EMBL:ADW67468.1};
OS   Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN   [1] {ECO:0000313|Proteomes:UP000000343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA   Haggblom M.M., Woyke T.;
RT   "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9.";
RL   Submitted (JAN-2011) 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; CP002480; ADW67468.1; -; Genomic_DNA.
DR   RefSeq; WP_013578796.1; NC_015064.1.
DR   AlphaFoldDB; E8WXD5; -.
DR   STRING; 1198114.AciX9_0396; -.
DR   PaxDb; 1198114-AciX9_0396; -.
DR   KEGG; acm:AciX9_0396; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_0; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000343; 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   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; 2.
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:ADW67468.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000343}.
FT   ACT_SITE        164
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        581
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   931 AA;  102259 MW;  8CC7FBE7201CCAA7 CRC64;
     MPSLWSPASW SSRLEELLSP AGELKGAPLR RDVRSLGMLL GLVLREQAAA GVYESVEGLR
     LAAIGRRESS DANAGALPSV AAEAADAGRA YQLARAFSFY FELINLAETN HRKRRRLAHQ
     LEDAAPQRGS LRGTLRALKK AGRSGEEIRE LLARVQVMAV FTAHPTEVAR RSVMFKRRRI
     SELLERLDGI PVPGATLEAL ERDLTAEITA LWQTDDVRAQ RPTVRDEIRM ALDYYESSLF
     DTLPVLYGEI EGALAAELGD KVELEDLPLL VTFGSWIGGD RDGNPFVTPA TTAEALGAAR
     ELLFGHYLKR LQTVFDQLGS STNQAGVTDE LEARLEVYLA ELRVAGSQSA EQRFVERFPQ
     ERVRLLVACM MLRLGGSPQS SVKLEAPPLA PYTAATELVG DLRVLRASLG AHHGERLAAM
     LIDPLVVEAK TYGLHLQALD IRQHARVHAA AIEELAGASD VAKVPEALSA GTMEVLETFQ
     MLAKLKREYP AESVARYVIS GATSAEDVLN VVRLARVGGV AVEGSESDPG LQPVPLFESI
     EDLQNAPAIC RELWGAAAYK PLLASWGGAQ EVMLGYSDSN KDGGMMTSTW EIFKAHRALY
     EVAAECGVTL RLFHGRGGTV GRGGGPTHRA IYAQPMDSFS GQLRLTEQGE VLNWKYSDVV
     LAERNLELMI AASLDALGRP KDKGEHLTGV LLPEWERVLD GLSESSYAFY RKHIVDDPET
     FTYFEQATPV AELEHARIGS RPAKRTDASS AKKRSMEDLR AIPWVFGWMQ SRHLVPAWFG
     VGHALALYEA EFGLDLLQKM FRSFPLFIDI VRNVEMALAK ADFGIARLYA SLVEDAGLRE
     RVLGTLEREF ELTTKMVLAV TGQSVLLERN AVLEQSIRLR NPYVDPLSLL QVELMRRKRG
     LGEADEVERG NIDRAITATI NGISAGLRNT G
//