ID   L0M8L8_ENTBF            Unreviewed;       883 AA.
AC   L0M8L8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 60.
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=D782_4406 {ECO:0000313|EMBL:AGB80269.1};
OS   Enterobacteriaceae bacterium (strain FGI 57).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB80269.1, ECO:0000313|Proteomes:UP000011002};
RN   [1] {ECO:0000313|EMBL:AGB80269.1, ECO:0000313|Proteomes:UP000011002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGI 57 {ECO:0000313|EMBL:AGB80269.1,
RC   ECO:0000313|Proteomes:UP000011002};
RX   PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA   Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA   Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA   Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA   Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA   Currie C.R.;
RT   "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT   associated with leaf-cutter ant fungus gardens.";
RL   Genome Announc. 1:E00238-12(2013).
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; CP003938; AGB80269.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0M8L8; -.
DR   STRING; 693444.D782_4406; -.
DR   KEGG; ebf:D782_4406; -.
DR   PATRIC; fig|693444.3.peg.4198; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000011002; 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:AGB80269.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011002}.
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;  99064 MW;  8BB61C857D667C52 CRC64;
     MNEQYSALRS NVSMLGKVLG DTIKDALGEN ILDRVETIRK LSKSSRAGNE ANRQELLTTL
     QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPKGEAASN PEVIARTLRK LKDQPNLTEA
     TIKKAVESLS LELVLTAHPT EITRRTLIHK MGEINGCLKQ LDNKDIADYE RHQLMRRLRQ
     LIAQSWHTDE IRKHRPSPVD EAKWGFAVVE NSLWEGVPNY LRELNEQLEE NLNYRLPVDF
     VPVRFTSWMG GDRDGNPNVT AEITRHVLLL SRWKATDLFL KDIQLLISEL SMVECTDELR
     ALVGEEGAQE PYRYLLKNIR SQLMATQSWL EARLKGQRLP KPAGLISQNE QLWDPLYACY
     KSLQACGMGI IANGELLDTL RRVKCFGVPL VRIDVRQEST RHTEALGELT RYLGIGDYES
     WSEADKQAFL IRELNSKRPL LPRSWEPSNE TREVLNTCKA IVDAPVGSVA AYVISMAKTP
     SDVLAVHLLL KEAGITFALP VAPLFETLDD LNNSNDVMTQ LLNIDWYRGF IQGKQMVMIG
     YSDSAKDAGV MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP
     PGSLKGGLRV TEQGEMIRFK YGLPEVTVSS LSLYTSAILE ANLLPPPEPK EEWRGIMDEL
     SDISCEMYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA
     WTQNRLMLPA WLGAGAALQK VVEDGKQSQL EAMCRDWPFF STRLGMLEMV FAKADLWLAE
     YYDQRLVKKE LWGLGEELRT LLEADIKVVL AIANDAHLMA DLPWIAESIQ LRNIYTDPLN
     VLQAELLHRS RLAEEEGKEP DPNVEQALMV TIAGVAAGMR NTG
//