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Database: UniProt/TrEMBL
Entry: A0A023V7F7_CITFR
LinkDB: A0A023V7F7_CITFR
Original site: A0A023V7F7_CITFR 
ID   A0A023V7F7_CITFR        Unreviewed;       883 AA.
AC   A0A023V7F7;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-SEP-2017, entry version 25.
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=CFNIH1_07375 {ECO:0000313|EMBL:AHY11341.1};
OS   Citrobacter freundii CFNIH1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=1333848 {ECO:0000313|EMBL:AHY11341.1, ECO:0000313|Proteomes:UP000025226};
RN   [1] {ECO:0000313|EMBL:AHY11341.1, ECO:0000313|Proteomes:UP000025226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFNIH1 {ECO:0000313|EMBL:AHY11341.1,
RC   ECO:0000313|Proteomes:UP000025226};
RA   Conlan S., Korlach J., Thomas P.J., Mullikin J., Frank K., Palmore T.,
RA   Segre J.A.;
RT   "Whole genome sequencing of Citrobacter freundii.";
RL   Submitted (APR-2014) 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; CP007557; AHY11341.1; -; Genomic_DNA.
DR   RefSeq; WP_038636064.1; NZ_CP007557.1.
DR   EnsemblBacteria; AHY11341; AHY11341; CFNIH1_07375.
DR   GeneID; 23336095; -.
DR   KEGG; cfd:CFNIH1_07375; -.
DR   KO; K01595; -.
DR   Proteomes; UP000025226; 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   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:UP000025226};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AHY11341.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AHY11341.1}.
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;  99144 MW;  7C8D9E84733E73A3 CRC64;
     MNEQYSALRS NVSMLGKVLG ETIKDALGEH ILDRVETIRK LSKSSRAGNE VNRQELLTTL
     QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPKGEAASN PEVIARTLRK LKDQPNLDEA
     TIKKAVESLS LELVLTAHPT EITRRTLIHK MGEVNTCLKQ LDNKDLVDYE RHQLMRRLRQ
     LIAQSWHTDE IRKIRPSPVD EAKWGFAVVE NSLWEGVPNY LRELNEQLEE NLGYKLPVDF
     VPVRFTSWMG GDRDGNPNVT ADITRHVLLL SRWKATDLFL KDIQFLISEL SMVDATPELL
     ALVGEEGAAE PYRYLMKTLR SRLMATQAWL EARLKGEKLP KPAGLLTQNE QLWDPLYACY
     QSLQACGMGI IANGELLDTL RRVKCFGVPL VRIDIRQEST RHTEALGELT RYLGIGDYEN
     WSEADKQAFL IRELNSKRPL LPRNWEPSND TREVLDTCRV IAEAPYGSIA AYVISMAKTP
     SDVLAVHLLL KEAGIGFAMP VAPLFETLDD LNNADDVMSQ LLNIDWYRGF IQGKQMVMIG
     YSDSAKDAGV MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP
     PGSLKGGLRV TEQGEMIRFK YGLPEVTISS LSLYTAAILE ANLLPPPEPK DNWRHIMDEL
     SDISCELYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA
     WTQNRLMLPA WLGAGTALQK VVEDGKQSEL EAMCRDWPFF STRLGMLEMV FAKADLWLAE
     YYDQRLVKKE LWPLGEELRQ RLAADIDVVL AIANDSHLMA DLPWIAESIQ LRNVYTDPLN
     VLQAELLHRS RLAEEQGNAP DPRVEQALMV TIAGVAAGMR NTG
//
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