ID   D5H069_LACCS            Unreviewed;       912 AA.
AC   D5H069;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 79.
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   ECO:0000313|EMBL:CBL51428.1};
GN   OrderedLocusNames=LCRIS_01981 {ECO:0000313|EMBL:CBL51428.1};
OS   Lactobacillus crispatus (strain ST1).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=748671 {ECO:0000313|EMBL:CBL51428.1, ECO:0000313|Proteomes:UP000002371};
RN   [1] {ECO:0000313|EMBL:CBL51428.1, ECO:0000313|Proteomes:UP000002371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST1 {ECO:0000313|EMBL:CBL51428.1,
RC   ECO:0000313|Proteomes:UP000002371};
RX   PubMed=20435723; DOI=10.1128/JB.00399-10;
RA   Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P.,
RA   Edelman S., Westerlund-Wikstrom B., Korhonen T.K., Paulin L., Kankainen M.;
RT   "Genome sequence of Lactobacillus crispatus ST1.";
RL   J. Bacteriol. 192:3547-3548(2010).
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; FN692037; CBL51428.1; -; Genomic_DNA.
DR   RefSeq; WP_013087066.1; NC_014106.1.
DR   AlphaFoldDB; D5H069; -.
DR   KEGG; lcr:LCRIS_01981; -.
DR   PATRIC; fig|748671.3.peg.1941; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000002371; 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:CBL51428.1}.
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        575
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   912 AA;  104429 MW;  CC7A8A588E95EE1E CRC64;
     MTVKKLENNS DVNVVAEESK VLTNLLNEST KQVIGQAAFD KIQNLIKISA AKDYQELEKQ
     IASLNNREMI VVARYFATLP LLINISEDVE LASKVNVLNN THQDYLGKLS DTIDIVAQKK
     NAEEILEHVN VVPVLTAHPT QVQRKTILEL TDQIHQLLRN YRDVKNGTID RDEWTEQMRA
     CIEILMQTDI IRGHKLKVAN EITNVLAYYP KALIPAITKF TSRYKELAKK HGLNASHATP
     ITMGMWIGGD RDGNPYVTAD TLELSATLQS QVIFEYYIKQ INKLYRAISM STSYMEPSDD
     VMHLSELSND DSPFRTNEPY RRAFYYIQSR LVHTEQKLLN ITNKNTFLKK RDLQNLDKIP
     CYQNAQEFKA DLEIIKNSLE EDHDHAVVDS YFTQILEAIN IFGFHLATID MRQDSSVNEA
     CVAELLKSAG ICDNYSDLSE DKKIKLLLNE LNNDPRNLHA NNKPKSELLQ KELKIYKTAR
     QLKDRLGEDV IKQHIISHTE SVSDMLEQAI MLKEYDLLDN QKARIQVVPL FETVEDLNNA
     REIIKEFLSF DIVKKWLVSQ NNYQEVMLGY SDSNKDGGYL ASCWNLYKAQ KDLTKIGEEM
     GIKITFMHGR GGTVGRGGGP SYEAITAQPF KSINDRMRMT EQGEIIQNKY GNKDTAYYNL
     EMLASATIDR MASKQIVSED HVADFRSSMD QIVAKSNEVY RKLVFENPNF LKYFFQATPI
     KEISGLNVGS RPASRKKLTD FSGLRAIPWV FSWSQSRVMF PGWYGVGSGF KSFIDADPAN
     LKELQNMYQG WPFFHSLLSN VDMVLSKSNM RIAKQYADLC EDEQIKSVFD IINQEWELTK
     KVILQIEGHD ELIEDAPTLK KSLEYRMPYF NILNYIQLEM IKRDREDEIQ GVYQSIIPIT
     INGVASGLRN SG
//