ID   B8ELY3_METSB            Unreviewed;       923 AA.
AC   B8ELY3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   04-NOV-2026, entry version 94.
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=Msil_1819 {ECO:0000313|EMBL:ACK50764.1};
OS   Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS   13906 / BL2).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Beijerinckiaceae; Methylocella.
OX   NCBI_TaxID=395965 {ECO:0000313|EMBL:ACK50764.1, ECO:0000313|Proteomes:UP000002257};
RN   [1] {ECO:0000313|EMBL:ACK50764.1, ECO:0000313|Proteomes:UP000002257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2
RC   {ECO:0000313|Proteomes:UP000002257};
RX   PubMed=20472789; DOI=10.1128/JB.00506-10;
RA   Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA   Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT   "Complete genome sequence of the aerobic facultative methanotroph
RT   Methylocella silvestris BL2.";
RL   J. Bacteriol. 192:3840-3841(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 = phosphoenolpyruvate +
CC         hydrogencarbonate; 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:ARBA00048995, 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; CP001280; ACK50764.1; -; Genomic_DNA.
DR   RefSeq; WP_012590834.1; NC_011666.1.
DR   AlphaFoldDB; B8ELY3; -.
DR   STRING; 395965.Msil_1819; -.
DR   KEGG; msl:Msil_1819; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OMA; AAAIPQC; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002257; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   NCBIfam; NF000584; ppc; 1.
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:ACK50764.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002257}.
FT   ACT_SITE        156
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        585
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   923 AA;  101856 MW;  646551DC70F06F09 CRC64;
     MTKVLDPISA NSASTIERPL IDDIRLLGQI LGDTIREQEG EDTFGLVEQA RRLSVEFERH
     ADPDAELKLN ELLRSLTPQQ AMAVIRAFSY FAHLANIAED RHNIRRRAAQ AAERPDEHDG
     GTLDKTFELL AAASITPEAV AEAIAQARVS PVLTAHPTEV QRRSLLDAER AIAQLLLARE
     TLSGERPRKQ NEMMLRARIA QLWQTRLLRY ARLSVRDEIE NSLAFYQMTF LKQIPQLYAR
     IEERLGSLPV ASFFRMGSWI GGDRDGNPNV NAGTLELALR RQCDTALRHY LREIHELGAE
     LSISGRLFGC AEALQELAEK SGDENPFRDD EPYRRALIGV YSRLSSTLTL LTGGEALRHA
     VAPGEPYANA GELQADLGVI EDSLRANHGA ALVPGRLGPL RRAVDVFGFH LASVDLRQSS
     DRHEETLKEL MSVARIVPDY SALDEDARQN LLIDLLRDPR PLRVPGVTYS PRTEEELEIF
     EAARDARRTF GEPAVVHYII SHTETVSDLL EVLALQKECG MVHGVLGEPG TSAELMVVPL
     FETIEDLRNA ATIMRGFYAL PGVAELTRAS GAEQEIMLGY SDSNKDGGFF TSNWELYRSS
     TALAALFKEH DGIALRLFHG RGGTVGRGGG PSYQAILAQP PGTVAGQIRL TEQGEVISSK
     YANPEIGLLN LEALVAATIE ATLLPSAGAA PKEFLDAAEE LSQASMKAFR AVIYDNPRFV
     DYFFTATPIA EIAELNIGSR PASRKSTRRI EDLRAIPWSF SWGQARINLP GWFGFGSAVE
     QFVAKAPAER MALLRRMGAE WPFFRALLSN MDMVLAKADM GLAGRYAELV PDQELAKSVF
     GSIEAEWART TKALNEITGV STRLSDNPAL AGAIKHRFPY ISPLNHLQVE LLRRWRSGEH
     DDKTLRSILI TINGVAAGLR NTG
//