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
//