ID   L0MMP7_9GAMM            Unreviewed;       881 AA.
AC   L0MMP7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=D781_4448 {ECO:0000313|EMBL:AGB84612.1};
OS   Serratia sp. FGI94.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=671990 {ECO:0000313|EMBL:AGB84612.1, ECO:0000313|Proteomes:UP000011001};
RN   [1] {ECO:0000313|EMBL:AGB84612.1, ECO:0000313|Proteomes:UP000011001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGI94 {ECO:0000313|EMBL:AGB84612.1,
RC   ECO:0000313|Proteomes:UP000011001};
RX   PubMed=23516234;
RA   Aylward F.O., Tremmel D.M., Starrett G.J., Bruce D.C., Chain P., Chen A.,
RA   Davenport K.W., Detter C., Han C.S., Han J., Huntemann M., Ivanova N.N.,
RA   Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M., Pagani I., Pati A.,
RA   Pitluck S., Teshima H., Deshpande S., Goodwin L., Woyke T., Currie C.R.;
RT   "Complete Genome of Serratia sp. Strain FGI 94, a Strain Associated with
RT   Leaf-Cutter Ant Fungus Gardens.";
RL   Genome Announc. 1:E0023912-E0023912(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; CP003942; AGB84612.1; -; Genomic_DNA.
DR   RefSeq; WP_015962308.1; NC_020064.1.
DR   AlphaFoldDB; L0MMP7; -.
DR   KEGG; smaf:D781_4448; -.
DR   PATRIC; fig|1249634.3.peg.4261; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000011001; 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:AGB84612.1}.
FT   ACT_SITE        137
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        545
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   881 AA;  98753 MW;  F626A7BB12FC3859 CRC64;
     MNEQYSAMRS NVSMLGKLLG ETIKEALGEH ILDRVETIRK LSKSSRAGNE AHRQELLTTL
     QNLSNDELLP VARAFSQFLN LTNVAEQYHS ISPHGEAASN PEAMAQLFSR LKGKKLSNKE
     LCDAVDQLSI ELVLTAHPTE ITRRTLIHKL VEVNTCLSQL DHNDLADYER NKIMRRLRQL
     VAQSWHTDEI RKNRPSPIDE AKWGFAVVEN SLWEGVPAFL REFNEQLENA IDYRLPVEAV
     PVRFTSWMGG DRDGNPNVTA EITRHVLLLS RWKACDLFTR DIQVLVSELS MTECTPALRE
     LAGGEAVQEP YREIMKRLRS QLVSSQAYLE GRLKGERMLK PHDLLVSNEQ LWEPLYACYQ
     SLVACGMGII ANGQLLDTLR RVRCFGVPLV RIDVRQESTR HTEAIAELTR YLGLGDYESW
     SEADKQAFLI RELNSKRPLV PLQWQPSADT QEVLETCRVI AEAPQGSIAA YVISMARTPS
     DVLAVHLLLK EAGCPFALPV APLFETLDDL NNADDVMTQL LSIDWYRGFI QGKQMVMIGY
     SDSAKDAGVM AASWAQYRAQ DALIKTCEKA GVALTLFHGR GGSIGRGGAP AHAALLSQPP
     GSLKGGLRVT EQGEMIRFKF GLPEVTISSL ALYTGAILEA NLLPPPEPKK EWRTLMDELS
     DTSCQMYRGY VRENPQFVPY FRAATPELEL GKLPLGSRPA KRRPNGGVES LRAIPWIFAW
     TQNRLMLPAW LGAGAGLQEA VKAGKQEQLA TMCRDWPFFS TRIAMLEMVF AKADLWLAEY
     YDQRLVDESL WPLGKQLREQ LESDIKVVLT IANDDNLMED LPWIAESIAL RNVYTDPLNV
     LQAELLHRSR QQEGSDQQDA RVEQALMVTI AGVAAGMRNT G
//