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Database: UniProt/TrEMBL
Entry: A0A0K0HH09_SALBC
LinkDB: A0A0K0HH09_SALBC
Original site: A0A0K0HH09_SALBC 
ID   A0A0K0HH09_SALBC        Unreviewed;       883 AA.
AC   A0A0K0HH09;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   28-MAR-2018, entry version 21.
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   ECO:0000313|EMBL:CCC32655.1};
GN   OrderedLocusNames=SBG_3610 {ECO:0000313|EMBL:CCC32655.1};
OS   Salmonella bongori (strain ATCC 43975 / DSM 13772 / NCTC 12419).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=218493 {ECO:0000313|EMBL:CCC32655.1, ECO:0000313|Proteomes:UP000000289};
RN   [1] {ECO:0000313|EMBL:CCC32655.1, ECO:0000313|Proteomes:UP000000289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43975 / DSM 13772 / NCTC 12419
RC   {ECO:0000313|Proteomes:UP000000289};
RX   PubMed=21876672; DOI=10.1371/journal.ppat.1002191;
RA   Fookes M., Schroeder G.N., Langridge G.C., Blondel C.J., Mammina C.,
RA   Connor T.R., Seth-Smith H., Vernikos G.S., Robinson K.S., Sanders M.,
RA   Petty N.K., Kingsley R.A., Baumler A.J., Nuccio S.P., Contreras I.,
RA   Santiviago C.A., Maskell D., Barrow P., Humphrey T., Nastasi A.,
RA   Roberts M., Frankel G., Parkhill J., Dougan G., Thomson N.R.;
RT   "Salmonella bongori provides insights into the evolution of the
RT   Salmonellae.";
RL   PLoS Pathog. 7:E1002191-E1002191(2011).
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; FR877557; CCC32655.1; -; Genomic_DNA.
DR   RefSeq; WP_001005552.1; NC_015761.1.
DR   STRING; 218493.SBG_3610; -.
DR   EnsemblBacteria; CCC32655; CCC32655; SBG_3610.
DR   KEGG; sbg:SBG_3610; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   BioCyc; SBON218493:G1H3O-3841-MONOMER; -.
DR   Proteomes; UP000000289; 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:UP000000289};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:CCC32655.1}.
FT   ACT_SITE    138    138       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    546    546       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   883 AA;  98949 MW;  93E9E739837F4946 CRC64;
     MNEQYSALRS NVSMLGKVLG ETIKDALGEH ILDRVETIRK LSKSSRAGNE ANRQELLTTL
     QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPKGEAASN PEVIARTLRK LKNQPDLNDA
     TIKKAVESLS LELVLTAHPT EITRRTLIHK MGEINNCLKQ LDNTDIADYE RHQVMRRLRQ
     LIAQSWHTDE IRKQRPSPVD EAKWGFAVVE NSLWQGVPNY LRELNEQLEE NLGYKLPVDF
     VPVRFTSWMG GDRDGNPNVT ADITRHVLLL SRWKATDLFL KDIQVLVSEL SMVDATPELL
     ARVGEEGASE PYRYLMKNLR ARLMATQSWL EARLKGEKLP KPAGLLTQNE QLWEPLYACY
     QSLQACGMGI IANGELLDTL RRVKCFGVPL VRIDIRQEST RHTEALGEIT RYLGIGDYES
     WSEADKQAFL IRELNSKRPL LPRNWEPSND TREVLETCKV IAEAPKGSIA AYVISMAKTP
     SDVLAVHLLL KEAGIGFAMP VAPLFETLDD LNNADDVMTQ LLNIDWYRGL IQGKQMVMIG
     YSDSAKDAGV MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP
     PGSLKGGLRV TEQGEMIRFK YGLPEVTVSS LSLYTSAILE ANLLPPPEPK DGWRHIMDEL
     SVISCQTYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA
     WTQNRLMLPA WLGAGTALQK VVEDGKQSEL EAMCRDWPFF STRLGMLEMV FSKADLWLAE
     YYDQRLVAKE LWPLGKELRD LLEEDIKVVL AIANDSHLMA DLPWIAESIQ LRNVYTDPLN
     VLQAELLHRS RLTEAQGKSP DPRVEQALMV TIAGVAAGMR NTG
//
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