ID   CAPP_LACDA              Reviewed;         909 AA.
AC   Q1GBD4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=Ldb0501;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS   / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS   00102 / Lb 14).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 /
RC   NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA   Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA   Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA   Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT   and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; CR954253; CAI97332.1; -; Genomic_DNA.
DR   RefSeq; WP_011543681.1; NC_008054.1.
DR   AlphaFoldDB; Q1GBD4; -.
DR   SMR; Q1GBD4; -.
DR   STRING; 390333.Ldb0501; -.
DR   KEGG; ldb:Ldb0501; -.
DR   PATRIC; fig|390333.7.peg.450; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   BioCyc; LDEL390333:LDB_RS02135-MONOMER; -.
DR   Proteomes; UP000001259; 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; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..909
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025563"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        572
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   909 AA;  103282 MW;  3A40C3CD76549A2F CRC64;
     MTAKKLENNS NHAVTAEEVK ILTDLLDEST RHLVGDEEFA KIKGLVKIAA SSDHSQLESQ
     IACLSNQEMI IVARYFATLP LLINITEDVD LATEVNLLNN TDKDYLGKLE STVDLVAEKD
     NAAEILSHVN VVPVLTAHPT QVQRKTILEL TNKIHDQLRR HRDVKASTIN RKEWTNQLRR
     YIEIIMQTDI IREKKLKVSN EIKNVMVYYP GSLIPAITKL TARYKELARE KGLNVDGATP
     ITMGMWIGGD RDGNPYVTAE TLRLSATIQS EVIFEYYVKA LNDLYRTVSV STSYVQPTPE
     VAELAKLSAD NSPFRENEPY RRAFYYLESR LAHTEMELLD VFSKEAVVKK EAALKAPVYK
     DAYEFKKDLE AIKRSLIQNH DRAVTGGHFD ALLEAIDVFG FHLATIDMRQ DSSVNEACVA
     ELLKSARICD NYSDLDEEEK IQILLSELNN DPRSLHSSNS PKSELLQREL KIYHTARLLK
     DTLGENVIKQ HIISHTESIS DMLEQAIMLK EYGLLDSEKA RVQVVPLFET VEDLQNSREI
     MKRYLSFDIV KRWVASKGNY QEIMLGYSDS NKDGGYLASC WNLYKAQTEL TAIGEEQGIK
     ITFMHGRGGT VGRGGGPSYE AITSQPFGSI KDRIRTTEQG EIIQNKYGNK DAAYYNLEML
     VSAAVDRMVS KQKVSQDHIQ DFTASMDGIV EDSNRVYREL VFDNPHFHDY FFQATPIKEV
     SSLNIGSRPA ARKKITELSG LRAIPWVFSW SQSRVMFPGW YGVGSAFKHF IDADPNNLKE
     LQEMYQGWPF FHSLLSNVDM VLSKSNMEIA EKYADLCEDE ATRSVFDIIK KEWELTKEVI
     LQIEGHSKLL EDNPSLERSL DYRLPYFNVL NYVQLEMIKR GRQEKLSGIY ESIIHITING
     VASGLRNSG
//