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Database: UniProt/TrEMBL
Entry: A0A1R2RSY2_SALEN
LinkDB: A0A1R2RSY2_SALEN
Original site: A0A1R2RSY2_SALEN 
ID   A0A1R2RSY2_SALEN        Unreviewed;       883 AA.
AC   A0A1R2RSY2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   25-OCT-2017, entry version 7.
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   ORFNames=ABA47_4091 {ECO:0000313|EMBL:KOX82090.1}, BCA92_22375
GN   {ECO:0000313|EMBL:ASD73894.1}, FORC52_4279
GN   {ECO:0000313|EMBL:ASL56191.1};
OS   Salmonella enteritidis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=149539 {ECO:0000313|EMBL:KOX82090.1, ECO:0000313|Proteomes:UP000037735};
RN   [1] {ECO:0000313|EMBL:KOX82090.1, ECO:0000313|Proteomes:UP000037735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LV60 {ECO:0000313|EMBL:KOX82090.1,
RC   ECO:0000313|Proteomes:UP000037735};
RA   Clemente L., Jones-Dias D., Egas C., Fookes M., Thomson N.R.,
RA   Manageiro V., Canica M.;
RT   "Draft genome sequence of a Salmonella Enteritidis strain from day-old
RT   chicks.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ASL56191.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FORC_052 {ECO:0000313|EMBL:ASL56191.1};
RG   Food-borne Pathogen Omics Research Center;
RA   Lee J.-H., Kim Y.-T., Ku H.-J., Kim H., Choi S.-H., Ryu S.;
RT   "Complete Genome Sequence of Salmonella enterica serovar Enteritidis
RT   FORC_052.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ASD73894.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CFSAN051873 {ECO:0000313|EMBL:ASD73894.1};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ASD73894.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CFSAN051873 {ECO:0000313|EMBL:ASD73894.1};
RA   Hoffmann M., Timme R., Sanchez M.;
RT   "Whole genome sequencing of cultured foodborne pathogen.";
RL   Submitted (JUN-2017) 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; CP022003; ASD73894.1; -; Genomic_DNA.
DR   EMBL; CP016754; ASL56191.1; -; Genomic_DNA.
DR   EMBL; LIHI01000009; KOX82090.1; -; Genomic_DNA.
DR   RefSeq; WP_001005548.1; NZ_NBRL01000011.1.
DR   KEGG; senl:IY59_20725; -.
DR   KO; K01595; -.
DR   Proteomes; UP000037735; Unassembled WGS sequence.
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:UP000037735};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:KOX82090.1}.
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;  99003 MW;  2F28CE22308A003E 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 KDIHVLVSEL SMVDATPELL
     ALVGEEGASE PYRYLMKKLR 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 DSWRHIMDEL
     SVISCETYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA
     WTQNRLMLPA WLGAGTALQK VVEDGKQSEL EAMCRDWPFF STRLGMLEMV FSKADLWLAD
     YYDQRLVAKT LWPLGKELRD LLEEDIKVVL AIANDSHLMA DLPWIAESIQ LRNVYTDPLN
     VLQAELLYRS RLTEEQGKSP DPRVEQALMV TIAGVAAGMR NTG
//
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