ID   E3EBK0_PAEPS            Unreviewed;       930 AA.
AC   E3EBK0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
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   Synonyms=pepC {ECO:0000313|EMBL:ADO58674.1};
GN   ORFNames=PPSC2_22145 {ECO:0000313|EMBL:ADO58674.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO58674.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO58674.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO58674.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT   growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT   activity.";
RL   J. Bacteriol. 193:311-312(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;
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; CP002213; ADO58674.1; -; Genomic_DNA.
DR   RefSeq; WP_013373240.1; NC_014622.2.
DR   AlphaFoldDB; E3EBK0; -.
DR   STRING; 1406.LK13_09635; -.
DR   KEGG; ppm:PPSC2_22145; -.
DR   PATRIC; fig|886882.15.peg.4714; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000006868; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT   ACT_SITE        153
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        587
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   930 AA;  106740 MW;  074F99B3FF3466A7 CRC64;
     MTELTLTANK NQSNNLLRRD VRFLGNILGE VLVHQGGNEL LDIVEKIREA SKSLRAGYQP
     ELYENFKQMV SGLDTDIRHQ VIRAFAIYFQ LVNIAEQNHR IRRKRDYEHS AGEEVQPGSI
     ESSVQELKQG GFSAEDVSNM LNELSLELVM TAHPTEATRR VILDIHKRIS EDVMLLDNPM
     LTLREREQVR ENLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETLFH VLPDVYQELE
     RCLVKYYPEQ KWHIPTYLRF GSWIGGDRDG NPSVTSHVTW ETLRMQRKLA LREYQHTLKE
     LMGYLSFSTS IVRVSDDLLA SIEEDRAHIT LKKMEVWHNE KEPYRIKLAY MIAKVNNVLD
     ESKQGTKERY SSAEELIADL NVIDNSLRHH FADYVADTYI QKMIRQVELF GFHTATLDVR
     QHSQEHENAM TEILSKMKIV SDYSKLSEEE KIDLLEQLLN EPRPITSPYL KYSDSTQECL
     DVYRTIYLAQ EEFGKQSITS YLISMTQGAS DLLEVMVLAK EVGLFRIEKD GTVICTLQSV
     PLFETIDDLH AAPDIMRRLM NLPVYRQSVA AMDELQEIML GYSDSNKDGG VVTANWELRV
     AMNSITEVVN EYGAKVKFFH GRGGALGRGG MPLNRSILAQ PPHTIGGGIK ITEQGEVLSS
     RYSLKGIAYR SLEQATSALI TAAAYHRSGK KEVFEESWEE IIARISEVSL EKYQDLIFRD
     PDFFSFFKES TPLPEVGELN IGSRPSKRKN SERFEDLRAI PWVFAWTQSR YLLPAWYAAG
     TGLQSYYQNN EDNLKVLQTM FRDSAFFRSL IDTLQMAIAK ADLLIAEEYA GMSDNEEARQ
     RIFGQISAEF KLTSELILKI TGQSEILDDV PVIQESIRLR NPYVDPLSYL QVQLLSELRE
     LRNQNGDDAE MLREVLLTIN GIAAGLRNTG
//