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Database: UniProt/TrEMBL
Entry: F2LZQ9_LACAL
LinkDB: F2LZQ9_LACAL
Original site: F2LZQ9_LACAL 
ID   F2LZQ9_LACAL            Unreviewed;       912 AA.
AC   F2LZQ9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
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=LAB52_05605 {ECO:0000313|EMBL:AEA32062.1};
OS   Lactobacillus amylovorus (strain GRL 1118).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=695562 {ECO:0000313|EMBL:AEA32062.1, ECO:0000313|Proteomes:UP000008140};
RN   [1] {ECO:0000313|EMBL:AEA32062.1, ECO:0000313|Proteomes:UP000008140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GRL 1118 {ECO:0000313|Proteomes:UP000008140};
RX   PubMed=21478337; DOI=10.1128/JB.00423-11;
RA   Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.;
RT   "Genome sequence of Lactobacillus amylovorus GRL1118, isolated from pig
RT   ileum.";
RL   J. Bacteriol. 193:3147-3148(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GRL 1118;
RA   Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.;
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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,
CC         ECO:0000256|HAMAP-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; CP002609; AEA32062.1; -; Genomic_DNA.
DR   RefSeq; WP_013641964.1; NC_017470.1.
DR   AlphaFoldDB; F2LZQ9; -.
DR   GeneID; 66523890; -.
DR   KEGG; lay:LAB52_05605; -.
DR   PATRIC; fig|695562.4.peg.1112; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000008140; 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:AEA32062.1}.
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;  104413 MW;  726990BEF20E4B12 CRC64;
     MTFTKLENSG DQAVVAEEVK ILTNLLNEST RQLIGDEKFA KIQDLINISA SKDQRQLEEK
     ISSLNNREMI VVARYFATLP LLINISEDVE LASKVNVFNN TDQDYLGKLS DTIDLVAKKD
     DAKRILENVN VVPVLTAHPT QIQRKTVLEL TDKIHHLLRS YRDGKNGTIN QKEWTEQLRA
     CIEILMQTDI IRGHKLKVSN EITNVLAYYP KALIPAITKF TARYKELAKE HDLTLDHATP
     ITMGMWIGGD RDGNPYVTAD TLELSATLQS QVIFEYYMKE LKKLYRAISL STSYMHPSAA
     VEKLSELSND DSPFRTNEPY RRAFYYIESR LVHTEKQLLG VVDKNIFIKP RDLENLENIP
     VYNDPQEFKA DLETIKASLD EDHDQAVTHS FFTEILEAID VFGFHLATID MRQDSSVNEA
     CVAELLKSAG ICDDYSDLSE DEKIKLLLNE LENDPRNLHA NNKPKSELLQ KELKIYKTAR
     QLKDRLGEDV IKQHIISHTE SVSDMLEQAV MLKEYDLLDN EKARVQVVPL FETVEDLLNA
     REIITEYLNF PIVKKWLASQ NNYQEIMLGY SDSNKDGGYL ASCWNLYKAQ RDLTAIGEKM
     GVKITYMHGR GGTVGRGGGP SYDAITAQPF KSINDRIRMT EQGEIIQNKY GNKDTAYYNL
     EMLASAAIDR MVSKQIVSED HIQDFRSSMD QIVDESNKIY RELVFENPAF LDYFFQATPI
     KEISNLNIGS RPASRKKLTD FSGLRAIPWV FSWSQSRIMF PGWYGVGSAF KHFIDADPAN
     LKELQEMYKG WPFFNSLLAN VDMVLSKSNM DIAREYANLC DDEETKKVFD IIYKEWKLTK
     KVILQIENHD ELLAEAPVLK QSLDYRMPYF NILNYIQIEM IKRGREDEIQ GVYHSIIPIT
     INGVASGLRN SG
//
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