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Database: UniProt/TrEMBL
Entry: D8P0A0_RALSL
LinkDB: D8P0A0_RALSL
Original site: D8P0A0_RALSL 
ID   D8P0A0_RALSL            Unreviewed;       986 AA.
AC   D8P0A0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-SEP-2017, entry version 51.
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   ECO:0000313|EMBL:CBJ50473.1};
GN   ORFNames=RPSI07_1114 {ECO:0000313|EMBL:CBJ50473.1};
OS   Ralstonia solanacearum PSI07.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=859657 {ECO:0000313|EMBL:CBJ50473.1, ECO:0000313|Proteomes:UP000006858};
RN   [1] {ECO:0000313|EMBL:CBJ50473.1, ECO:0000313|Proteomes:UP000006858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PSI07 {ECO:0000313|EMBL:CBJ50473.1,
RC   ECO:0000313|Proteomes:UP000006858};
RX   PubMed=20550686; DOI=10.1186/1471-2164-11-379;
RA   Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E.,
RA   Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G.,
RA   Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.;
RT   "Genomes of three tomato pathogens within the Ralstonia solanacearum
RT   species complex reveal significant evolutionary divergence.";
RL   BMC Genomics 11:379-379(2010).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595}.
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; FP885906; CBJ50473.1; -; Genomic_DNA.
DR   RefSeq; WP_013211812.1; NC_014311.1.
DR   EnsemblBacteria; CBJ50473; CBJ50473; RPSI07_1114.
DR   KEGG; rsl:RPSI07_1114; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000006858; 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:UP000006858};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:CBJ50473.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:CBJ50473.1}.
FT   ACT_SITE    193    193       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    635    635       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   986 AA;  108850 MW;  DB35222BCEB7839F CRC64;
     MTQPAARRAS SRATPARKTP PAPASQAKAP SANGAAGTAL GPTSRRSSGS AAAKDQPLKE
     DIRFLGRLLG DVLREQEGAA AFETVETIRQ TAVRFRRDGD KQAEQELDRL LKTLSRDQTT
     SVVRAFSYFS HLANIAEDQH HNRRRRVHAL ASSPPQPGSL LRALLSVADE GLSGEALRRF
     FDAALIVPVL TAHPTEVQRK SILDAQREIA RLLAERDAPL TARERERNTA LLRAHVTKLW
     QTRMLRTTRL MVSDEIENAL SYYQTTFLRE IPALYRELEE DVATVFPRRG ARGEPAPLPA
     FFQMGSWIGG DRDGNPFVTA QTLRHAAQRQ ASVILTWYLD EIHALGAELS MSTSLVDVSA
     ELLALAERSP DHSEHRADEP YRRALIGVYA RLAATCRELT GEDAGRHAVG PAPAYTSAED
     LRTDIQVVID SLAAHHGEAL TDARLTSLAR AIDVFGFHLA SIDLRQVSDV HEATVAELLK
     VAGVEGAYAA LSEADKRTLL LRELQQPRLL TLPFHAYSET TASELDIFRA AREVRARYGN
     RIVRNYIISH TETLSDLLEV MLLQKEAGMF RHGHNGGGGG AGLHVMVIPL FETIEDLRNA
     PQIMGDLLAL PGFDAVLAAQ GNEQEVMLGY SDSNKDGGFL TSNWELYKAE LALVELFERK
     GAHLRLFHGR GGTVGRGGGP TYQAILSQPP GTVNGQIRLT EQGEIISSKF ANPEIGRRNL
     ETIVAATLEA TMLPTRNRPK GLEEFEAAMQ ALSDHAFAAY RHLVYETPGF KDYFFATTPI
     TEIADLNLGS RPASRKLMDK KHRRIEDLRA IPWGFSWGQC RLLLPGWFGF GSAVQRWLDE
     AGNAKAKAAR LATLKRMHKQ WPFFANLLSN MDMVLSKADL NVASRYAQLC DDRKLRNAVF
     SRISAEFTLT EQVLAAITGQ SERLADNPLL ARSIKNRFPY LDPLNHLQVE LLKRFRSGKA
     GSDDARVRRG IHLSINGIAA GLRNSG
//
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