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Database: UniProt/TrEMBL
Entry: A0A089MED1_9BACL
LinkDB: A0A089MED1_9BACL
Original site: A0A089MED1_9BACL 
ID   A0A089MED1_9BACL        Unreviewed;       930 AA.
AC   A0A089MED1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-SEP-2017, entry version 25.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
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|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=R70331_28145 {ECO:0000313|EMBL:AIQ54984.1};
OS   Paenibacillus sp. FSL R7-0331.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ54984.1, ECO:0000313|Proteomes:UP000029487};
RN   [1] {ECO:0000313|EMBL:AIQ54984.1, ECO:0000313|Proteomes:UP000029487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ54984.1,
RC   ECO:0000313|Proteomes:UP000029487};
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
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; CP009284; AIQ54984.1; -; Genomic_DNA.
DR   RefSeq; WP_042181025.1; NZ_CP009284.1.
DR   EnsemblBacteria; AIQ54984; AIQ54984; R70331_28145.
DR   KEGG; paee:R70331_28145; -.
DR   KO; K01595; -.
DR   Proteomes; UP000029487; 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   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   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029487};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AIQ54984.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029487}.
FT   ACT_SITE    153    153       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    587    587       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   930 AA;  106507 MW;  FE89FDE3747E8043 CRC64;
     MTELTTAVSK SNSNNLLRRD VRFLGNILGE VLVHQGGNEL LEVVEKIRET SKSLRSLFLP
     ELHNEFKELI SSLDPENRHQ VIRAFAIYFQ LVNIAEQNHR IRRKRDYERS AGDTVQPGSI
     ESAIQELRER DFSQEDVHDI MNNLSLELVM TAHPTEAMRR AILDIHKRIS DDVMGLDNPT
     LTFREREQLR EKLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETIFQ VLPDVYQELE
     RCLSKYYPGQ NWHVPTYLRF GSWIGGDRDG NPSVTAAVTM QTLRLQRKLA IREYQRIMRE
     LMQYLSFSTS IVSVTDELLD SIEQDRGIIK LNRVDAWRND NEPYRIKLSY MISKTQNVLD
     DERKGTPERY ATPQQFIDDL NVIDRSLRHH FADYVADTYI KKLIRQVELF GFHTAALDVR
     QHSQEHENAM AEILAKMNIT QDYAKMPEDQ KVTLLESILN DPRPLTSPYQ SYSESTEECL
     AVYRTVYLAQ EEYGKQCITS YLISMAEAAS DILEVMVFSK EVGLFRKDND GTVVCTLQAV
     PLFETIDDLH NAPQIMKTLL SMPIYREAVR AMNDLQEIML GYSDSNKDGG VVTANWELRV
     ALKQITATAD EFGIKLKFFH GRGGALGRGG MPLNRSILAQ PASTIGGGIK ITEQGEVISS
     RYSMQGIAYR SLEQATSALV TAAIHARTPQ ADLYEAKWDE IVARISEVSL TKYQDLIFRD
     PDFLSFFKES TPLPEVGELN IGSRPSKRKN SDRFEDLRAI PWVFAWTQSR YLLPAWYAAG
     TGLQSFYEGK EENMKIMQTM YADFSFFTTL IDTLQMAIAK ADLVIAKEYA SMGKNDEARQ
     RIFGQIQAEF KLTSELILKI TGQHEILDNV PVIQESIRLR NPYVDPLSYL QVQLLSELRV
     LRDAEGDDAE LLREVLLTIN GIAAGLRNTG
//
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