ID E0J693_ECOLW Unreviewed; 883 AA.
AC E0J693;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
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|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN ECO:0000313|EMBL:ADT77618.1};
GN OrderedLocusNames=ECW_m4312 {ECO:0000313|EMBL:ADT77618.1};
OS Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC
OS 13500 / NCIMB 8666 / NRRL B-766 / W).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=566546 {ECO:0000313|EMBL:ADT77618.1, ECO:0000313|Proteomes:UP000008525};
RN [1] {ECO:0000313|EMBL:ADT77618.1, ECO:0000313|Proteomes:UP000008525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 /
RC NCIMB 8666 / NRRL B-766 / W {ECO:0000313|Proteomes:UP000008525};
RX PubMed=21208457; DOI=10.1186/1471-2164-12-9;
RA Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y.,
RA Nielsen L.K.;
RT "The genome sequence of E. coli W (ATCC 9637): comparative genome analysis
RT and an improved genome-scale reconstruction of E. coli.";
RL BMC Genomics 12:9-9(2011).
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC ECO:0000256|HAMAP-Rule:MF_00595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC Evidence={ECO:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC Rule:MF_00595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00595};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR EMBL; CP002185; ADT77618.1; -; Genomic_DNA.
DR RefSeq; WP_001005603.1; NZ_WBMH01000045.1.
DR AlphaFoldDB; E0J693; -.
DR KEGG; elw:ECW_m4312; -.
DR PATRIC; fig|566546.30.peg.4381; -.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000008525; 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 Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_00595};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595}.
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 546
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 883 AA; 99091 MW; 138B92CC1F6A22CE CRC64;
MNEQYSALRS NVSMLGKVLG ETIKDALGEH ILERVETIRK LSKSSRAGNE ANRQELLTTL
QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPKGEAASN PEVIARTLRK LKNQPELSED
TIKKAVESLS LELVLTAHPT EITRRTLIHK MVEVNACLKQ LDNKDIADYE HNQLMRRLRQ
LIAQSWHTDE IRKLRPSPVD EAKWGFAVVE NSLWQGVPNY LRELNEQLEE NLGYKLPVEF
VPVRFTSWMG GDRDGNPNVT ADITRHVLLL SRWKATDLFL KDIQVLVSEL SMVEATPELL
ALVGEEGAAE PYRYLMKNLR SRLMATQAWL EARLKGEELP KPEGLLTQNE ELWEPLYACY
QSLQACGMGI IANGDLLDTL RRVKCFGVPL VRIDIRQEST RHTEALGELT RYLGIGDYES
WSEADKQAFL IRELNSKRPL LPRNWQPSAE TREVLDTCQV IAEAPQGSIA AYVISMAKTP
SDVLAVHLLL KEAGIGFAMP VAPLFETLDD LNNANDVMTQ LLNIDWYRGL IQGKQMVMIG
YSDSAKDAGV MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP
PGSLKGGLRV TEQGEMIRFK YGLPEITVSS LSLYTGAILE ANLLPPPEPK ESWRRIMDEL
SVISCDLYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA
WTQNRLMLPA WLGAGTALQK VVEDGKQSEL EAMCRDWPFF STRLGMLEMV FAKADLWLAE
YYDQRLVDKA LWPLGKELRN LQEEDIKVVL AIANDSHLMA DLPWIAESIQ LRNIYTDPLN
VLQAELLHRS RQAEKEGQEP DPRVEQALMV TIAGIAAGMR NTG
//