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Database: UniProt/TrEMBL
Entry: E0RFW4_PAEP6
LinkDB: E0RFW4_PAEP6
Original site: E0RFW4_PAEP6 
ID   E0RFW4_PAEP6            Unreviewed;       930 AA.
AC   E0RFW4;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-SEP-2017, entry version 50.
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   OrderedLocusNames=PPE_04220 {ECO:0000313|EMBL:ADM72000.1};
OS   Paenibacillus polymyxa (strain E681).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=349520 {ECO:0000313|EMBL:ADM72000.1, ECO:0000313|Proteomes:UP000002227};
RN   [1] {ECO:0000313|EMBL:ADM72000.1, ECO:0000313|Proteomes:UP000002227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E681 {ECO:0000313|EMBL:ADM72000.1,
RC   ECO:0000313|Proteomes:UP000002227};
RX   PubMed=20851896; DOI=10.1128/JB.00983-10;
RA   Kim J.F., Jeong H., Park S.Y., Kim S.B., Park Y.K., Choi S.K.,
RA   Ryu C.M., Hur C.G., Ghim S.Y., Oh T.K., Kim J.J., Park C.S.,
RA   Park S.H.;
RT   "Genome sequence of the polymyxin-producing plant-probiotic
RT   rhizobacterium Paenibacillus polymyxa E681.";
RL   J. Bacteriol. 192:6103-6104(2010).
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; CP000154; ADM72000.1; -; Genomic_DNA.
DR   RefSeq; WP_013312130.1; NC_014483.2.
DR   STRING; 349520.PPE_04220; -.
DR   EnsemblBacteria; ADM72000; ADM72000; PPE_04220.
DR   KEGG; ppy:PPE_04220; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000002227; 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:UP000002227};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ADM72000.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ADM72000.1}.
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;  106949 MW;  BAC8682A132AD690 CRC64;
     MTELTLTANK NQSNNLLRRD VRFLGNILGE VLVHQGGNEL LDIVEKIRET SKSLRAGYQP
     ELYENFKQMV SGLDTDIRHQ VIRAFAIYFQ LVNIAEQNHR IRRKRDYEHS AGEDVQPGSI
     ESSVQELKQE GFSAEDVSNL LKELSLELVM TAHPTEATRR VILDIHKRIS EDVMLLDNPM
     LTLREREQVR ENLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETLFH VLPDVYQELE
     RCLDKYYPEQ KWHIPTYLRF GSWIGGDRDG NPSVTAHVTW ETLRMQRKLA LREYQHTLKE
     LMGYLSFSTS IVRVSDDLLA SIEEDRTHIT LKKMEVWHNE KEPYRIKLAY MIAKVNNTLD
     ESKQGTNERY NSAEELIADL NVIDNSLRHH FADYVANTYI QKMIRQVELF GFHTATLDVR
     QHSQEHENAM TEILSKMNIV SDYSKLSEEE KINLLEKLLN EPRPITSPYL KYSDSTQECL
     DVYRTIYLAQ EEFGKQSITS YLISMTQGAS DLLEVMVLSK EVGLFRIEKD GTVICTLQSV
     PLFETIDDLH AAPDIMRRLM NLPVYRQSVA AMDQLQEIML GYSDSNKDGG VVTANWELRV
     AMNSITEVVN EFGVKVKFFH GRGGALGRGG MPLNRSILAQ PPHTIGGGIK ITEQGEVLSS
     RYSLRGIAYR SLEQATSALI TAVAYHRSGK KEVFEESWED IIARISQVSL DKYQDLIFRD
     PDFFNFFKES TPLPEVGELN IGSRPSKRKN SERFEDLRAI PWVFAWTQSR YLLPAWYAAG
     TGLQSFYQNN EDNLKVLQTM FRDSAFFRSL IDTLQMAIAK ADLLIAEEYA GMSDNEEARQ
     RIFGQISAEF KLTSELILKI TGQSEILDDV PVIQESIRLR NPYVDPLSYL QVQLLSELRE
     LRDQNGDDTE MLREVLLTIN GIAAGLRNTG
//
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