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Database: UniProt/TrEMBL
Entry: Q12SN2_SHEDO
LinkDB: Q12SN2_SHEDO
Original site: Q12SN2_SHEDO 
ID   Q12SN2_SHEDO            Unreviewed;       887 AA.
AC   Q12SN2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 89.
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=Sden_0248 {ECO:0000313|EMBL:ABE53544.1};
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE53544.1, ECO:0000313|Proteomes:UP000001982};
RN   [1] {ECO:0000313|EMBL:ABE53544.1, ECO:0000313|Proteomes:UP000001982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013
RC   {ECO:0000313|Proteomes:UP000001982};
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., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-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; CP000302; ABE53544.1; -; Genomic_DNA.
DR   RefSeq; WP_011494711.1; NC_007954.1.
DR   ProteinModelPortal; Q12SN2; -.
DR   STRING; 318161.Sden_0248; -.
DR   EnsemblBacteria; ABE53544; ABE53544; Sden_0248.
DR   KEGG; sdn:Sden_0248; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000001982; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP.
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:UP000001982};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ABE53544.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ABE53544.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001982}.
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;  99877 MW;  98319488DEC8371D CRC64;
     MSVQSKAEDA TDVYASLRAN VGQLGQILGD TMRSHLGDAF LEKVEQIRIL AKKSRQGDDG
     AREQMLALLT ALPDEELIPF AKAFNQFLNL ANIAEQFHTI SRNCDELVCV PDPVEQLLGR
     LLKHDLDKSQ LHQCLTELDI DLVLTAHPTE ISRRTLIQKY ASVVDCLTSL ENPLLTEREH
     SQLQLRLRQL IAQIWHTNEI RHERPTPVDE ARWGLSTIET SLWQAVPDFL RQLNDQFEQK
     TGLQLAKDVS PVRFSSWMGG DRDGNPFVTA RVTQEVLDRN RHAAARLYLK DIVTLMNELS
     MEEANAELKA LTNNSNEPYR DVLKGLRQKL RNTIDYLNER LEGHQPDIDF NSIIWEQSDL
     QAPLECLYQS LCDSGMRLIA HGLLLDILRR LACFGIHMLK LDIRQDAERH SDVIAELTRY
     LGLGDYHHWD EDEKQAFLLR ELTNRRPLLP PNWKPSPDVA EVLSTCALIS KQSPKALGSY
     VISMASKPSD VLTVLLLLKE SGCTYPMRVV PLFETLKDLT GAAACIKELL QIDWYRGYTK
     GMQEVMIGYS DSAKDAGVMA AAWAQYRAQE ELVAVCKQAG VKLTLFHGRG GTVGRGGGPA
     HQAILSQPPG SVDGRIRVTE QGEMIRFKFG LPKLAVQSLA LYTSAVMEAT LMPPPEPKKA
     WRECMQAIAD ESVLAYRGIV REEPDFVAYF RAATPEVELG KLPLGSRPAK RKVGGGIESL
     RAIPWIFAWS QNRLMLPAWL GAGEALSSAI EQSQLNLLQE MEREWPFFET RISMLEMVYT
     KAEPNLARYY ERCLVPTELH HLGDKLRARL QLGIDTVLSL TQSDELMSHT PWSRESVKLR
     NPYIDPLNFL QTELLARTRN EDQASEKVQL ALMLTIAGVA AGMRNTG
//
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