ID A0A172TG80_9BACL Unreviewed; 929 AA.
AC A0A172TG80;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SY83_05725 {ECO:0000313|EMBL:ANE45887.1};
OS Paenibacillus swuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE45887.1, ECO:0000313|Proteomes:UP000076927};
RN [1] {ECO:0000313|EMBL:ANE45887.1, ECO:0000313|Proteomes:UP000076927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6 {ECO:0000313|EMBL:ANE45887.1,
RC ECO:0000313|Proteomes:UP000076927};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Paenibacillus swuensis/DY6/whole genome sequencing.";
RL Submitted (JAN-2015) 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; CP011388; ANE45887.1; -; Genomic_DNA.
DR RefSeq; WP_068605114.1; NZ_CP011388.1.
DR AlphaFoldDB; A0A172TG80; -.
DR STRING; 1178515.SY83_05725; -.
DR KEGG; pswu:SY83_05725; -.
DR PATRIC; fig|1178515.4.peg.1161; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000076927; 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:ANE45887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076927}.
FT ACT_SITE 153
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 586
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 929 AA; 106511 MW; EA35BB3AF017BE97 CRC64;
MSEVAVVTSK NQPNNLLRRD VRFLGNILGE VLVHQGGTEL LDIVEKIREM SKSLRANYVP
SLFEEFKNTI RGLDSENRHQ VIRAFAIYFQ LVNIAEQNHR IRRKRDYERT SGENIQPGSI
ESVIVELKDS NISIEEVQEL LEGISLELVM TAHPTEAMRR AVLAIHKRIA DDVMLLDNPT
ITYREREQLR EKLLNEVITL WQTDELRDRK PTVVDEVRNG MYYFDETLFN ALPDVYQELE
RCLDKYYPEH AWHVPTYLRF GSWIGGDRDG NPSVTAKVTW ETLKMHRQLV LRKYEEILKH
LMGLLSFSTN LIEISPELAE SIRKDREQVE TRNIDMWRNE REPYRIKLSF MREKLFNTKV
EGISPEAKYN NADELIQDLK IIDRSLRNHF ADYVADTELK KTIRQVELFG FHLVALDVRQ
HSKEHENAMA EILAHMNIVK NYPELTEEAK IELLHELLKD PRPLTSPYAQ YTPSTQECLD
VYVTIQAAQK EFGVGCISSY LISMTQGASD LLEVMVFAKE VGLYRKDAEG NVVCTLQSVP
LFETIDDLHE APAIMDTLFQ IPAYKQGVEA MNGQQEIMLG YSDSNKDGGM ITANWELRVA
LNEITNTGNA HGVKLKFFHG RGGALGRGGM PLNRSILAQP PHTLGGGIKI TEQGEVLSSR
YAMQPIAYRS LEQATSALIT AALLAKYPQS NAQEEQWNEI IKEISEVAQK KYQDLIFRDP
DFLTFFKEST PLPEIGELNI GSRPSKRKNS DRFEDLRAIP WVFSWTQSRY LLPAWYAAGT
ALQSYYEGNE EKLKILQQMY AKSSFFRTMI DSLQMALAKA DLIIAKEYAN MIKDKTTEQR
IFGGIQEEYK VTSELIMLIT GQQDILDNVP VIQESIRLRN PYVDPLSYMQ VQLITELRAL
REQGEDDPDL LREVLLTING IAAGLRNTG
//
