ID A0A089JZA2_9BACL Unreviewed; 930 AA.
AC A0A089JZA2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=H70737_27095 {ECO:0000313|EMBL:AIQ26179.1};
OS Paenibacillus sp. FSL H7-0737.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ26179.1, ECO:0000313|Proteomes:UP000029519};
RN [1] {ECO:0000313|EMBL:AIQ26179.1, ECO:0000313|Proteomes:UP000029519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ26179.1,
RC ECO:0000313|Proteomes:UP000029519};
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; CP009279; AIQ26179.1; -; Genomic_DNA.
DR RefSeq; WP_042192083.1; NZ_CP009279.1.
DR AlphaFoldDB; A0A089JZA2; -.
DR KEGG; paej:H70737_27095; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_9; -.
DR Proteomes; UP000029519; 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:AIQ26179.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029519}.
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; 106978 MW; D7C47B243B02B7BC CRC64;
MTELTTTVSK SNSNNLLRRD VRFLGNILGE VLVHQGGNEL LEIVEKIRET SKSLRSLFLP
ELHSEFKELI NSLDPENRHQ VIRAFAIYFQ LVNIAEQNHR IRRKRDYERS AGETVQPGSI
ESAIKELRER DFSHEEVNEI IAGLSLELVM TAHPTEAMRR AILDIHKRIS DDVMGLDNPT
LTFREREQLR EKLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETIFH VLPDVYQELE
RCLSKYYPGQ NWHVPTYLRF GSWIGGDRDG NPSVTSTVTS QTLRMQRKLA IREYQRIMRE
LMKYLSFSTS IVKVTPELVE SIEADREIIN LGKMEEWRND NEPYRIKLSY MISKTQNVLD
DEKKDTLERY STPEEFIDDL NVIDRSLRHH YADYVADTYI KKLIRQVELF GFHTATLDVR
QHSQEHENAM TEILAKMNIT PDYSKLSEDE KIELLEKLLN DPRPITSSYQ TYSEGTEECL
AVYRTIFASQ EEYGKQCITS YLISMAEAAS DILEVMVFSK EVGLFRKDND GTVVCTLQAV
PLFETIDDLH EAPQIMNRLL SMPIYRDAVR AMNDLQEIML GYSDSNKDGG VVTANYELRV
ALKEITATAD KFGIKLKFFH GRGGALGRGG MPLNRSILAQ PASTIGGGIK ITEQGEVISS
RYSMQGIAYR SLEQATSALV TAAINARIPQ ADLYEEKWEE IVARISEVSL HKYQDLIFRD
PDFLTYFKES TPLPEVGELN IGSRPSKRKN SDRFEDLRAI PWVFAWTQSR YLLPAWYAAG
TGLQSFYEGK EENLKIMQHM YENFSFFTTL IDTLQMAISK ADLIIAKEYA SMGKNEEARQ
RIFGQIEDEF KLTSELILKI TGQQDILDNV PVIQESIRLR NPYVDPLSYL QVQLLSELRA
LREIDGDDSE LLREVLLTIN GIAAGLRNTG
//