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Database: UniProt/TrEMBL
Entry: A0A089MFK4_9BACL
LinkDB: A0A089MFK4_9BACL
Original site: A0A089MFK4_9BACL 
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
//
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