ID E2X3C7_SHIDY Unreviewed; 883 AA.
AC E2X3C7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
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 ORFNames=Asd1617_04984 {ECO:0000313|EMBL:AHA67811.1};
OS Shigella dysenteriae 1617.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=754093 {ECO:0000313|EMBL:AHA67811.1, ECO:0000313|Proteomes:UP000031647};
RN [1] {ECO:0000313|EMBL:AHA67811.1, ECO:0000313|Proteomes:UP000031647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1617 {ECO:0000313|EMBL:AHA67811.1,
RC ECO:0000313|Proteomes:UP000031647};
RA Aksomboon Vongsawan A., Kapatral V., Vaisvil B., Serichantalergs O.,
RA Hale T.L., Mason C.J.;
RT "Comparative genomics of Sd1617 to representative strains in evaluating its
RT pathogenesis.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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; CP006736; AHA67811.1; -; Genomic_DNA.
DR RefSeq; WP_001005574.1; NZ_ADUT01000007.1.
DR AlphaFoldDB; E2X3C7; -.
DR SMR; E2X3C7; -.
DR KEGG; sdz:Asd1617_04984; -.
DR PATRIC; fig|754093.4.peg.4849; -.
DR HOGENOM; CLU_006557_2_0_6; -.
DR Proteomes; UP000031647; 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};
KW Pyruvate {ECO:0000313|EMBL:AHA67811.1}.
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT ACT_SITE 546
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 883 AA; 99093 MW; 466E1EE722AB50C5 CRC64;
MNEQYSALRS NVSMLGKVLG ETIKDALGEH ILERVETIRK LSKSSRAGND 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 ANLLPPPELK ESWRRIMDEL
SVISCDLYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA
WTQNRLMLPA WLGAGTALQK VVEDGKQSEL EAMCRDWPFF STRLGMLEMV FAKADLWLAE
YYDQRLVDKA LWPLGKELRN LQEEDIKVVL AIANDSHLMA DLPWIAESIQ LRNIYTDPLN
VLQAELLHRS RQAEKEGQEP DPRVEQALMV TIAGIAAGMR NTG
//
