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
//