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Database: UniProt/TrEMBL
Entry: A0A089JZA2_9BACL
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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
//
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