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Database: UniProt/TrEMBL
Entry: A3DA27_SHEB5
LinkDB: A3DA27_SHEB5
Original site: A3DA27_SHEB5 
ID   A3DA27_SHEB5            Unreviewed;       889 AA.
AC   A3DA27;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   22-NOV-2017, entry version 83.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Sbal_4125 {ECO:0000313|EMBL:ABN63590.1};
OS   Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN63590.1, ECO:0000313|Proteomes:UP000001557};
RN   [1] {ECO:0000313|EMBL:ABN63590.1, ECO:0000313|Proteomes:UP000001557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557};
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., Sims D.R., Brettin T., Bruce D., Han C., Tapia R.,
RA   Brainard J., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Brettar I., Klappenbach J., Konstantinidis K.,
RA   Rodrigues J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS155.";
RL   Submitted (FEB-2007) 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:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
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:SAAS00946753}.
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DR   EMBL; CP000563; ABN63590.1; -; Genomic_DNA.
DR   RefSeq; WP_011848139.1; NC_009052.1.
DR   ProteinModelPortal; A3DA27; -.
DR   STRING; 325240.Sbal_4125; -.
DR   EnsemblBacteria; ABN63590; ABN63590; Sbal_4125.
DR   KEGG; sbl:Sbal_4125; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000001557; 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   PANTHER; PTHR30523; PTHR30523; 1.
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:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001557};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ABN63590.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ABN63590.1}.
FT   ACT_SITE    146    146       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    553    553       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   889 AA;  100307 MW;  58E2CDD5D92C5B0A CRC64;
     MVVTKADNMT DMYASLRSNV SMLGQILGDT MRTHLGDSFL EKVEQIRKLA KDSRRGDQAA
     REQMLELLTA LPDEELVPFA KAFNQFLNLA NLSEQFHTIS RNCDELVCVP DPVEQLLGRM
     LNGRVDQTKM LDCLKTLDID LVLTAHPTEI SRRTLIQKYA AIVDCLTEQE NDQLSDRERQ
     QISLRLRQLI AQIWHTNEIR RERPTPVDEA RWGLSTIEES LWHAVPDFLR QLNDQVQQRT
     GQQLPIDIAP VRFSSWMGGD RDGNPFVTAK VTQEVLDRNR HAAARLFLKD IVLLVGELSM
     EEANDELKAY TNNSCEPYRH VLRSIRQRLR DTIDYLNARI EGHNPEVDKS SLIWQESDLK
     APLEMLYKSL TDCGMRLIAN GLLLDILRRL ACFGIHMLRL DIRQDASRHS DVLAELTRYL
     GMGDFNHWDE TEKQAFLLRE LSNRRPLIPS NWQPSADVAE VLNTCRLIAK HPAKALGSYV
     ISMAGKPSDV LTVLLLLKET GCSHPMRVVP LFETLSDLNN AAACITDLLD IDWYRGYTKG
     MQEVMIGYSD SAKDAGVMAA AWAQYHAQEQ LVAVCKQAGV KLTLFHGRGG SIGRGGGPAH
     KAILSQPPGS VDGRIRVTEQ GEMIRFKFGL PKLAVQSLAL YTSAVLEATL LPPPEPKQQW
     RDCMQRIAEE SVGAYRGIVR DEPDFVAYFR AATPEVELGK LPLGSRPAKR RVDGGIESLR
     AIPWIFAWSQ NRLMLPAWLG AGEALQAASE RGEMGLLQDM EREWPFFSTR ISMLEMVYAK
     AEPNLARYYE TCLVPKDLHH LGETLRQRLD LGIKVVLELT KSDSLMAHTP WNRESVKLRN
     PYIDPLNFLQ TELLARTRKE TTETPASEHV QLALMLTIAG VAAGMRNTG
//
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