ID A0A1G5L7Z4_9BACL Unreviewed; 930 AA.
AC A0A1G5L7Z4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN05720606_12173 {ECO:0000313|EMBL:SCZ09073.1};
OS Paenibacillus polysaccharolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=582692 {ECO:0000313|EMBL:SCZ09073.1, ECO:0000313|Proteomes:UP000198538};
RN [1] {ECO:0000313|EMBL:SCZ09073.1, ECO:0000313|Proteomes:UP000198538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL9 {ECO:0000313|EMBL:SCZ09073.1,
RC ECO:0000313|Proteomes:UP000198538};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FMVM01000021; SCZ09073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5L7Z4; -.
DR STRING; 582692.SAMN05720606_12173; -.
DR Proteomes; UP000198538; Unassembled WGS sequence.
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:SCZ09073.1}.
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; 106347 MW; A5ED528295E38C77 CRC64;
MTETTVTASK SQSNNLLRRD VRFLGNILGE VLVHQGGTEL LDVVEKIRET SKSLRAEFLP
ELYEEFKTMI QELDSDNRHQ VIRAFAIYFQ LVNIAEQNHR IRRKRDYERS AGDAVQPGSI
EKAVQDLKER GLSHTEVEEI LDDLSLELVM TAHPTEAMRR VILDIHKRIS EDVMLLDNPT
LTLREREQLR EKLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETLFH VLPDVYQELE
RCLNKFYPDH DWHVPTYLRF GSWIGGDRDG NPSVTSDVTW QTLLMQRKLA LREYQRIMIE
LMGHLSFSTN IIHISDELAQ SIEQDRNCVT LKKVDIWRNE KEPYRIKLAY MIAKLNNVLD
ENKVGQPDRY QNAQDLIDDL LIIDRSLRHH FADYVADTTV RKMIRQVELF GFHTAALDVR
QHSKEHESAM SEILAKMNIV DDYARLTEDG KIDLLARLLD DPRPLTSPYH QYTEGTRECL
DVFRAIKRAQ NEFGTSCITS YLISMTQGAS DLLEVMVFAK EVGLFSKGAN GEVISTLQAV
PLFETIDDLH AASEIMQRLF NLPIYRASVT GRNELHEIML GYSDSNKDGG VVTANWELRV
AMNAITAVGN EHGVKLKFFH GRGGALGRGG MPLNRSILAQ PPHTIGGGIK ITEQGEVISS
RYSLQGIAYR SLEQATSALI TAALNGLEPQ ESASEQAWDE IIKDISEVSL TKYQDLIFRD
PDFFTFFKES TPLPEVGELN IGSRPSKRKG SDKFEDLRAI PWVFAWTQSR YLLPAWYAAG
TGLQSYYQGK EENLNVLKEM YANFPFFRTL IDTVQMAVAK ADLVIAKEYS AMTSNKEARD
RIFGQIESEF KLTKELILKI TGEAEILDDV PVIQESIRLR NPYVDPLSYM QVQLLSELRD
MRERGEDDTE LLREVLLTIN GIAAGLRNTG
//
