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Database: UniProt/TrEMBL
Entry: A0A089IDR6_9BACL
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ID   A0A089IDR6_9BACL        Unreviewed;       930 AA.
AC   A0A089IDR6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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   ORFNames=H70357_31495 {ECO:0000313|EMBL:AIQ20703.1};
OS   Paenibacillus sp. FSL H7-0357.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536774 {ECO:0000313|EMBL:AIQ20703.1, ECO:0000313|Proteomes:UP000029508};
RN   [1] {ECO:0000313|EMBL:AIQ20703.1, ECO:0000313|Proteomes:UP000029508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0357 {ECO:0000313|EMBL:AIQ20703.1,
RC   ECO:0000313|Proteomes:UP000029508};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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,
CC         ECO:0000256|HAMAP-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; CP009241; AIQ20703.1; -; Genomic_DNA.
DR   RefSeq; WP_038600882.1; NZ_CP009241.1.
DR   AlphaFoldDB; A0A089IDR6; -.
DR   STRING; 1536774.H70357_31495; -.
DR   KEGG; paeh:H70357_31495; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000029508; 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   Pyruvate {ECO:0000313|EMBL:AIQ20703.1}.
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;  106952 MW;  7235C6531A2B38FD CRC64;
     MTELTTTVSK SNSNNLLRRD VRFLGNILGE VLVHQGGNEL LEIVEKIRET SKSLRSLFLP
     ELHNEFKELI NSLDPENRHL VIRAFAIYFQ LVNIAEQNHR IRRKRDYERS AGETVQPGSI
     ESAIQELRER DFSHEDVHEI MNGLSLELVM TAHPTEAMRR AILDIHKRIS DDVMGLDNPT
     LTFREREQLR EKLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETIFQ VLPDVYQELE
     RCLSKYYPGQ NWHVPTYLRF GSWIGGDRDG NPSVTAAVTL QTLRLQRKLA IREYQRIMRE
     LMQYLSFSTS IVEVTQELVD SIEQDRNIIN LNRVDAWRND NEPYRIKLSY MISKIQNVLD
     DEKKGTPERY SSPERFIDDL NVIDRSLRHH YADYVADTYI KKLIRQVELF GFHTATLDVR
     QHSQEHENAM TEILAKMNIT QDYAKLEENE KIRILENLLN DPRPLTSPYQ TYSESTEECL
     AVYRTIFTAQ EEYGKQCITS YLISMAEAAS DILEVMVFAK EVGLFRKDND GTVVCTLQAV
     PLFETIDDLH DAPQIMRTLL SMPIYRDAVS AMSDVQEIML GYSDSNKDGG VVTANWELRV
     ALKQITATAE EFGIKLKFFH GRGGALGRGG MPLNRSILAQ PASTIGGGIK ITEQGEVISS
     RYSMQGIAYR SLEQATSALV TAAINARMPE ADLYESKWEE IVARISEVSL NKYQDLIFRD
     PDFFAYFKES TPLPEVGELN IGSRPSKRKN SDRFEDLRAI PWVFAWTQSR YLLPAWYAAG
     TGLQSFYEDK EENLKIMQHM YENFSFFTTL IDTLQMAIAK ADLIIAKEYA SMGKNEEARQ
     RIFGQIEAEF KLTSELILKI TGQQDILDNV PVIQESIRLR NPYVDPLSYL QVQLLSELRA
     LREVEGDDAE LLREVLLTIN GIAAGLRNTG
//
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