ID   E3G4Q0_ENTLS            Unreviewed;       883 AA.
AC   E3G4Q0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
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   OrderedLocusNames=Entcl_4285 {ECO:0000313|EMBL:ADO50518.1};
OS   Enterobacter lignolyticus (strain SCF1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pluralibacter.
OX   NCBI_TaxID=701347 {ECO:0000313|EMBL:ADO50518.1, ECO:0000313|Proteomes:UP000006872};
RN   [1] {ECO:0000313|Proteomes:UP000006872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCF1 {ECO:0000313|Proteomes:UP000006872};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H.,
RA   Hazen T.C., Woyke T.;
RT   "Complete sequence of Enterobacter cloacae SCF1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO50518.1, ECO:0000313|Proteomes:UP000006872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCF1 {ECO:0000313|EMBL:ADO50518.1,
RC   ECO:0000313|Proteomes:UP000006872};
RX   PubMed=22180812; DOI=10.4056/sigs.2104875;
RA   Deangelis K.M., D'Haeseleer P., Chivian D., Fortney J.L., Khudyakov J.,
RA   Simmons B., Woo H., Arkin A.P., Davenport K.W., Goodwin L., Chen A.,
RA   Ivanova N., Kyrpides N.C., Mavromatis K., Woyke T., Hazen T.C.;
RT   "Complete genome sequence of "Enterobacter lignolyticus" SCF1.";
RL   Stand. Genomic Sci. 5:69-85(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, ECO:0000256|HAMAP-
CC         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; CP002272; ADO50518.1; -; Genomic_DNA.
DR   RefSeq; WP_013368228.1; NC_014618.1.
DR   AlphaFoldDB; E3G4Q0; -.
DR   STRING; 701347.Entcl_4285; -.
DR   KEGG; esc:Entcl_4285; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000006872; 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   Reference proteome {ECO:0000313|Proteomes:UP000006872}.
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;  98800 MW;  AAE3571B7310E4C5 CRC64;
     MNEQYSALRS NVSMLGKVLG ETIKDALGEN ILDRVETIRK LSKSSRAGNE ANRQELLTTL
     QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPNGEAASN PEVIARTLRK LKDQPELNDA
     TIKKAVESLS LELVLTAHPT EITRRTLIHK MVEVNSCLKQ LDNKDIADYE RHQLMRRLRQ
     LIAQSWHTDE IRKLRPSPVD EAKWGFAVVE NSLWEGVPNY LRELNEQLEA NLGYRLPVDF
     VPVRFTSWMG GDRDGNPNVT ADITRHVLLL SRWKATDLFL KDVQVLISEL SMVEATPELR
     ALAGAEGEQE PYRHLMKNLR SQLMATQTWL EARLKGEKLP KPAGLLTQNE QLWEPLYACY
     KSLQACGMGI IANGELLDTL RRVKCFGVPL VRIDIRQEST RHTEALGELT RYLGIGDYES
     WSEADKQAFL IRELNSKRPL LPRQWEPSDE TREVLDTCKV IAEAPKGSIA AYVISMAKTP
     SDVLAVHLLL KEAGIGFALP VAPLFETLDD LNNANDVMTQ LLNIDWYRGF IQGKQMVMIG
     YSDSAKDAGV MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP
     PGSLKGGLRV TEQGEMIRFK YGLPEVTISS LSLYTSAILE ANLLPPPEPK AEWRHIMNEL
     SDVSCKMYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA
     WTQNRLMLPA WLGAGAALQQ VVAGGKQSEL ETMCRDWPFF STRLGMLEMV FSKADLWLAE
     YYDQRLVTKA LWPLGAELRK LLEGDIKVVL DIANDSHLMA DLPWIAESIQ LRNIYTDPLN
     VLQAELLHRS RQAEEAGEAP DPRVEQALMV TIAGVAAGMR NTG
//