ID A0A089MFK4_9BACL Unreviewed; 930 AA.
AC A0A089MFK4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=PGRAT_28890 {ECO:0000313|EMBL:AIQ71160.1};
OS Paenibacillus graminis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=189425 {ECO:0000313|EMBL:AIQ71160.1, ECO:0000313|Proteomes:UP000029500};
RN [1] {ECO:0000313|EMBL:AIQ71160.1, ECO:0000313|Proteomes:UP000029500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15220 {ECO:0000313|EMBL:AIQ71160.1,
RC ECO:0000313|Proteomes:UP000029500};
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; CP009287; AIQ71160.1; -; Genomic_DNA.
DR RefSeq; WP_025705073.1; NZ_CP009287.1.
DR AlphaFoldDB; A0A089MFK4; -.
DR STRING; 189425.PGRAT_28890; -.
DR KEGG; pgm:PGRAT_28890; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_9; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000029500; 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:AIQ71160.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029500}.
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; 106792 MW; 1C6536E802D0EB3A CRC64;
MTELTTAVSK SNSNNLLRRD VRFLGNILGE VLVHQGGNEL LEIVEKIRET SKSLRSLFLP
ELHNEFKELI NSLDPENRHQ VIRAFAIYFQ LVNIAEQNHR IRRKRDYERS AGETVQPGSI
ESAIQELRER DFSHEDVHEI MNGLSLELVM TAHPTEAMRR AILDIHKRIS DDVMGLDNPT
LTFREREQLR EKLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETIFQ VLPDVYQELE
RCLSKYYPGQ NWHVPTYLRF GSWIGGDRDG NPSVTAAVTL QTLRLQRKLA IREYQRIMRE
LMQYLSFSTS IVKVTPELLE SIELDRGIIQ LDKTKSWHND NEPYRIKLTY MIAKTQNVMD
DEKKGSLERY SSPEQFIDDL NVIDRSLRHH YADYVADTYI KKLIRQVELF GFHTATLDVR
QHSQEHENAM TEILAKMNVT QDYAKLQENE KIELLEKLLN DPRPLTSPYQ TYSESTEECL
AVYRTIYTAQ EEYGKQCITS YLISMAEAAS DILEVMVFSK EVGLFRKDND GTVVCTLQAV
PLFETIDDLH DAPQIMRTLL NLPIYRDAVR AMNDLQEIML GYSDSNKDGG VVTANYELRV
ALKEITATAD EFGIKLKFFH GRGGALGRGG MPLNRSILAQ PASTIGGGIK ITEQGEVISS
RYSMQGIAYR SLEQATSALI TAAINARSPQ ADLYDPKWEE IVARISEVSL NKYQDLIFRD
PDFLNYFKES TPLPEVGELN IGSRPSKRKN SDRFEDLRAI PWVFAWTQSR YLLPAWYAAG
TGLQSFYDGK EENLKIMQHM YEEFSFFTTL IDTLQMAIAK ADLIIAKEYA GMGKNEEARH
RIFGQIEAEF KLTSELILKI TGQQDILDNV PVIQESIRLR NPYVDPLSYL QVQLLSELRA
LREAEGDDAE LLREVLLTIN GIAAGLRNTG
//