ID   D5DB23_PRIM3            Unreviewed;       922 AA.
AC   D5DB23;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 77.
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=BMD_0812 {ECO:0000313|EMBL:ADF37674.1};
OS   Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=592022 {ECO:0000313|EMBL:ADF37674.1, ECO:0000313|Proteomes:UP000002365};
RN   [1] {ECO:0000313|EMBL:ADF37674.1, ECO:0000313|Proteomes:UP000002365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 319 / IMG 1521 {ECO:0000313|Proteomes:UP000002365};
RX   PubMed=21705586; DOI=10.1128/JB.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Huot Creasy H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
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; Evidence={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; CP001982; ADF37674.1; -; Genomic_DNA.
DR   RefSeq; WP_013081842.1; NZ_CP120609.1.
DR   AlphaFoldDB; D5DB23; -.
DR   KEGG; bmd:BMD_0812; -.
DR   PATRIC; fig|592022.4.peg.729; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000002365; 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; 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.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:ADF37674.1}.
FT   ACT_SITE        152
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        579
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   922 AA;  105986 MW;  E41A4A8FAF278B70 CRC64;
     MVTVEAAERQ NSSTALRRDV KFLGQLLGKV LVHQGGEELL SKVEKIREVA KSLRENKDEV
     IYKEIKNEIV TLEQPMREQV IRAFAVYFHL VNIAEQNHRI RRRREYQQQE DSIMQPGSLE
     SAVVSLKNNG VAPDVIANLL QTLSLELIIT AHPTEATRRS VLDIHKRMAE LLKNLDNPTL
     TKRERTEIEE RLFSEVLILW QTNELRDRKP TVMDEVSNGL YYFDETLFEV LPQLHQELEN
     SLQENYPEEN WKVPNILRFG SWIGGDRDGN PNVTPKVTWQ TLVKQRKLAI RKYKESLTQL
     RQRLSQSTKR VAVSDNLLDS INQEISLLPE KKRWRIKHEV YRCKLTIMLH KLNLVGESEA
     GYQRSEELLH DLFLIKDSLQ KHQPQDYQLK SLCKLIRQVE LFGFHLATLD IRNHSGEHEA
     AIKEIFHAVS LAEDYSALTE EKKVELLGKV LQDPRPVISF VENYSKETQQ VIEVFNMIHR
     AHKEFGERSI EVYLISMTQS ASDLLEVMVL AKEAGIYRLH ADGRIESKLN IAPLLETIDD
     LTAGPKIMEQ LFQLDFYREH LREQQDLQEI MLGYSDGSKD GGTLTANWKL YKAQQEIHDM
     AKKYQVRLKF FHGRGGSLGR GGGPLNRSIL SQPVETLGDG VKITEQGEVL SSRYALYDIA
     YRSLEQAVSA LLTAAANVSQ EAEQCDIRTH EWEETMDEIS TASLRKYQEL VFKDPDFLTY
     FKQATPLPEL GALNIGSRPM SRKGSDRFED LRAIPWVFAW TQSRQLLPAW YAAGTGLQHL
     VEKSGDIQLL QQMYKEWPFF RSTVDNLQMA LTKADLMAAK EYTEMVQDPA ISERIFTAIK
     KEYNLTKEMI LQITGQKELM DHLPTIKESI KLRNPYVDPL TFLQVKVISK LREDEAGTLN
     EELLKEALLT INGIAAGLRN TG
//