ID   B2IBS4_BEII9            Unreviewed;       932 AA.
AC   B2IBS4;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
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=Bind_0138 {ECO:0000313|EMBL:ACB93796.1};
OS   Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS   8712).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Beijerinckia.
OX   NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB93796.1, ECO:0000313|Proteomes:UP000001695};
RN   [1] {ECO:0000313|Proteomes:UP000001695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC   {ECO:0000313|Proteomes:UP000001695};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA   Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT   "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT   9039.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACB93796.1, ECO:0000313|Proteomes:UP000001695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC   {ECO:0000313|Proteomes:UP000001695};
RX   PubMed=20601475; DOI=10.1128/JB.00656-10;
RA   Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C.,
RA   Dunfield P.F.;
RT   "Complete genome sequence of Beijerinckia indica subsp. indica.";
RL   J. Bacteriol. 192:4532-4533(2010).
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; CP001016; ACB93796.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2IBS4; -.
DR   STRING; 395963.Bind_0138; -.
DR   KEGG; bid:Bind_0138; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001695; 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:ACB93796.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001695}.
FT   REGION          112..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        594
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   932 AA;  103141 MW;  C7A9403A0E6B6EA3 CRC64;
     MTTKGARTDI MTNLARQADD RLNEEIRLLG QILGETIREQ EGDESFDRIE TIRRLSVAFE
     RGADAAAGET LDTLLRGLSA EQAVSVIRSF SYFSHLANIA EDHETIRRSI AETGTEEPAG
     QETDSADDDF DGGMARLTAA GVDKARIIEA LRQSFLSPVL TAHPTEVQRK SQLDAEHAIF
     SLLVEREHLG PGAARRRNDA LLAACITQAW QTRLLRNAKL TVRDEIENAL SYYQTTFLRQ
     LPALYAELEE WLGVRDLPCF LRMGSWIGGD RDGNPNVNAE TLDIALRRQA EVALRHYLSE
     VRALGNELSL SRLLVGCSQD LLRLAETSGD DSPHRADEPY RRALIAIKGR LAATLKELTG
     QEDSKPAPLG TQAYPDASAL LADLAIIEKS LAENHGRALI GPRLAPFQRA VKVFGFHLAT
     VDLRQSSDRH AETIGELLRV AKVVEDYDAL DEKARQDLLM RLLQDPRLLH VPYLRYSART
     EEELAVFETA RRLRRSHGPL AIRQYIISHT ETVSDLLEVL LLQKECGLIE GLIGDPEQKP
     RAELMVVPLF ETIEDLRNAQ GIMADFFALP GMADLVRASG GVQEIMLGYS DSNKDGGFFT
     SNWELYRVSI ALAGFFAAQE GIVLRLFHGR GGTIGRGGGP SHQAILAQPP GTANGLIRLT
     EQGEVISSKY AQPEIGRRNL ETLVAANIEA TLLGGDEAPP EAFLEAAHFL SEASTKAYRG
     LVYDLPGFVD YFYAATPIAE IADLNIGSRP ASRKSSRKIE DLRAIPWSFS WGQARVSLPG
     WFGFGTAVEA FLNDAPEEKL ALLQRMAREW PFFHALLSNM DMVLAKADRK LARRYAALVP
     DQALAERIFG IIDTEWTRTL HALDEITGVH ERLADNPALA HSISRRFPYI APLNHLQVEL
     LRRWRLGKTD ARTYNGILIS INGIAAGLRN SG
//