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Database: UniProt/TrEMBL
Entry: B5F0U5_SALA4
LinkDB: B5F0U5_SALA4
Original site: B5F0U5_SALA4 
ID   B5F0U5_SALA4            Unreviewed;       912 AA.
AC   B5F0U5;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   28-MAR-2018, entry version 71.
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:ACH50907.1};
GN   OrderedLocusNames=SeAg_B4360 {ECO:0000313|EMBL:ACH50907.1};
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH50907.1, ECO:0000313|Proteomes:UP000008819};
RN   [1] {ECO:0000313|EMBL:ACH50907.1, ECO:0000313|Proteomes:UP000008819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483 {ECO:0000313|EMBL:ACH50907.1,
RC   ECO:0000313|Proteomes:UP000008819};
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(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; CP001138; ACH50907.1; -; Genomic_DNA.
DR   EnsemblBacteria; ACH50907; ACH50907; SeAg_B4360.
DR   KEGG; sea:SeAg_B4360; -.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000008819; 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:UP000008819};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ACH50907.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ACH50907.1}.
FT   ACT_SITE    167    167       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    575    575       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   912 AA;  102539 MW;  5BB626D5DE8C851E CRC64;
     MTWVGERSQR RRSVKDAGQL QQRWGVWDHM NEQYSALRSN VSMLGKVLGE TIKDALGEHI
     LDRVETIRKL SKSSRAGNEA NRQELLTTLQ NLSNDELLPV ARAFSQFLNL ANTAEQYHSI
     SPKGEAASNP EVIARTLRKL KNQPDLNDAT IKKAVESLSL ELVLTAHPTE ITRRTLIHKM
     GEINNCLKQL DNTDIADYER HQVMRRLRQL IAQSWHTDEI RKQRPSPVDE AKWGFAVVEN
     SLWQGVPNYL RELNEQLEEN LGYKLPVDFV PVRFTSWMGG DRDGNPNVTA DITRHVLLLS
     RWKATDLFLK DIHVLVSELS MVDATPELLA LVGEEGASEP YRYLMKKLRA RLMATQSWLE
     ARLKGEKLPK PAGLLTQNEQ LWEPLYACYQ SLQACGMGII ANGELLDTLR RVKCFGVPLV
     RIDIRQESTR HTEALGEITR YLGIGDYESW SEADKQAFLI RELNSKRPLL PRNWEPSNDT
     REVLETCKVI AEAPKGSIAA YVISMAKTPS DVLAVHLLLK EAGIGFAMPV APLFETLDDL
     NNADDVMTQL LNIDWYRGLI QGKQMVMIGY SDSAKDAGVM AASWAQYQAQ DALIKTCEKA
     GIELTLFHGR GGSIGRGGAP AHAALLSQPP GSLKGGLRVT EQGEMIRFKY GLPEVTVSSL
     SLYTSAILEA NLLPPPEPKD SWRHIMDELS VISCETYRGY VRENKDFVPY FRSATPEQEL
     GKLPLGSRPA KRRPTGGVES LRAIPWIFAW TQNRLMLPAW LGAGTALQKV VEDGKQSELE
     AMCRDWPFFS TRLGMLEMVF SKADLWLADY YDQRLVAKTL WPLGKELRDL LEEDIKVVLA
     IANDSHLMAD LPWIAESIQL RNVYTDPLNV LQAELLYRSR LTEEQGKSPD PRVEQALMVT
     IAGVAAGMRN TG
//
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