ID   CAPP_LACH4              Reviewed;         912 AA.
AC   A8YVD9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
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};
GN   OrderedLocusNames=lhv_1193;
OS   Lactobacillus helveticus (strain DPC 4571).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=405566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 4571;
RX   PubMed=17993529; DOI=10.1128/jb.01295-07;
RA   Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA   McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA   Beresford T., Ross R.P.;
RT   "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT   selective gene loss and IS element expansion.";
RL   J. Bacteriol. 190:727-735(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000517; ABX27226.1; -; Genomic_DNA.
DR   RefSeq; WP_012211903.1; NC_010080.1.
DR   AlphaFoldDB; A8YVD9; -.
DR   SMR; A8YVD9; -.
DR   KEGG; lhe:lhv_1193; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000000790; 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.
FT   CHAIN           1..912
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000072623"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        575
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   912 AA;  104678 MW;  02ED016883C51F17 CRC64;
     MTVKKLENSS DVNVVTEEVK ILTNLLNEST EQLIGKELFT KIQNLIKISA DKNYQELEDQ
     IASLDNREMI VVARYFATLP LLINISEDVE LASKVNVLNN TNQDYLGKLN DTIDIVAQKK
     NAKEILEKVN VVPVLTAHPT QVQRKTVLEL TDKIHKLLRN YREVKNGIIT RVEWTEELRA
     CIEILMQTDI IRSHKLKVSN EITNVLTYYP KSLIPAITKF TARYKELAKK HGLDIPDATP
     ITMGMWIGGD RDGNPYVTAD TLKLSATLQG QVIFEYYIKQ INQLYRSISL STSYMKPSTE
     VMHLSELSND DSPFRTNEPY RRAFYYIESR LVRSEQKLLN ITNQHSFLKE RDLEHLDQIP
     AYEDAQEFKA DLEVIKRSLE ENRDQAVVKS YFTEILEAID VFGFHLATID MRQDSSVNEA
     CVAELLKSAE ICDHYSELSE KEKVSLLLNE LNNDPRNLHT NNKPKSELLQ KELKIYKTAR
     DLKDRLGEDL IKQHIISHTE SVSDMLEQAI MLKEYDLLDN QSARVQVVPL FETVEDLNNA
     RDIIKEYLNL DIVKKWLVSQ HNYQEVMLGY SDSNKDGGYL ASCWNLYKAQ KDLTAIGEEL
     GIKITYMHGR GGTVGRGGGP SYEAITAQPF NSINDRIRMT EQGEIIQNKY GNKDAAYYNL
     EMLVSATVDR IASKQIVSEE YIADFRSSMD KIVTESNEIY KKLVFENPNF LDYFLQATPI
     KEISNLNIGS RPASRKKLSD FSSLRAIPWV FSWSQSRVMF PGWYGVGSAF KHFIDADKKN
     LQELQHMYQG WPFFHALLSN ADMVLSKSNM EIAKQYAELC QDEKTKSVFD IIYQEWKLTK
     QIILQIEGHD DLLSDAPNLK NSLASRMPYF NILNYIQLEM IKRDREDEIK GVFQSIIPIT
     INGVASGLRN SG
//