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Database: UniProt/TrEMBL
Entry: A1S259_SHEAM
LinkDB: A1S259_SHEAM
Original site: A1S259_SHEAM 
ID   A1S259_SHEAM            Unreviewed;       887 AA.
AC   A1S259;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-SEP-2017, entry version 83.
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=Sama_0254 {ECO:0000313|EMBL:ABL98465.1};
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297 {ECO:0000313|EMBL:ABL98465.1, ECO:0000313|Proteomes:UP000009175};
RN   [1] {ECO:0000313|EMBL:ABL98465.1, ECO:0000313|Proteomes:UP000009175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Fredrickson J., Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
RL   Submitted (DEC-2006) 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; CP000507; ABL98465.1; -; Genomic_DNA.
DR   RefSeq; WP_011758375.1; NC_008700.1.
DR   ProteinModelPortal; A1S259; -.
DR   STRING; 326297.Sama_0254; -.
DR   EnsemblBacteria; ABL98465; ABL98465; Sama_0254.
DR   KEGG; saz:Sama_0254; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000009175; 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:UP000009175};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ABL98465.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ABL98465.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009175}.
FT   ACT_SITE    147    147       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    554    554       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   887 AA;  99321 MW;  548A59E60C0BA35D CRC64;
     MTDVKGTEKV TDMYAQLRAN VGMMGQILGD TMKEHLGEAF LDKVEQIRLL AKGSRSGDDE
     ARAKMLALLG QLPDEELVPF AKAFNQFLNL ANIAEQFHTI SRNCDELVCV PDPVEQLLGR
     MLGSQVDKKE MLATLKTLDI DLVLTAHPTE ISRRTLIQKY SAIVDCLHDL ENPQLTEREH
     KSQTLRLRQL IAQIWHTNEI RRERPTPVDE ARWGLSTIET SLWHAVPDFL RQLNDQVEEA
     TGTQIPTDMA PVRFSSWMGG DRDGNPFVTA RVTAEVLDRN RHTAARLYLK DVVELVGELS
     MEEANAELMA YSNNSCEPYR DVLRSLRSKL RNTIDFLNAR LEGHNPEVAR DEIIWEQQDL
     ETPLKLLYKS LCDSGMRLIA NGRLLDMLRR LACFGIHMLR LDIRQDAGRH EAAIAELTRY
     LGLGDYAHWS EAEKQAFLLK ELSGRRPLIP GNWKPSDEVA EVLATCRLVG TQPQQALGSY
     VISMASLPSD VLAVLLLLKE SGCNYPIRVV PLFETLDDLN NAAACITALL DIDWYRGYTK
     GMQEVMIGYS DSAKDAGVMA AAWAQYRAQE QLVKVCNKAG VKLTLFHGRG GTIGRGGGPA
     HKAILSQPPG SVDGRIRVTE QGEMIRFKFG LPKLAVQSLA LYTSAVLEAT LLPPPEPKQE
     WRNAMQRIAD ESVEAYRGIV RQEPDFVPYF RAATPEVELG KLPLGSRPAK RRVDGGIESL
     RAIPWIFAWS QNRLMLPAWL GAGEALKAAA DRGELGLLRE MEQDWPFFNT RISMLEMVYS
     KAEPNLARYY EQCLVPEALH HLGVTLRERL ALGVEAVLAL TGEDSLMAHT PWNRESVRLR
     NPYIDPLNFL QAELLGRTRR EETPSESVQL ALMLTIAGVA AGMRNTG
//
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