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Database: UniProt/TrEMBL
Entry: W5XY82_9CORY
LinkDB: W5XY82_9CORY
Original site: W5XY82_9CORY 
ID   W5XY82_9CORY            Unreviewed;       924 AA.
AC   W5XY82;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   ORFNames=CCASEI_02725 {ECO:0000313|EMBL:AHI19128.1};
OS   Corynebacterium casei LMG S-19264.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1285583 {ECO:0000313|EMBL:AHI19128.1, ECO:0000313|Proteomes:UP000019226};
RN   [1] {ECO:0000313|EMBL:AHI19128.1, ECO:0000313|Proteomes:UP000019226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG S-19264 {ECO:0000313|EMBL:AHI19128.1,
RC   ECO:0000313|Proteomes:UP000019226};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "The complete genome sequence of Corynebacterium casei LMG S-19264 (=DSM
RT   44701).";
RL   Submitted (FEB-2013) 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|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; CP004350; AHI19128.1; -; Genomic_DNA.
DR   RefSeq; WP_025387079.1; NZ_CP004350.1.
DR   AlphaFoldDB; W5XY82; -.
DR   STRING; 1285583.CCASEI_02725; -.
DR   GeneID; 82876738; -.
DR   KEGG; ccg:CCASEI_02725; -.
DR   PATRIC; fig|1285583.3.peg.528; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000019226; 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; 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.
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:AHI19128.1}.
FT   ACT_SITE        139
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        587
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   924 AA;  102193 MW;  DDD583FF490E88C8 CRC64;
     MSEQVRDDIR LLGRILGRVI AEQEGEDVYE LVESTRRLAF GVARGEEDAE ALLSTFRDVD
     ENKINLVARS FSHFALMANI AEDLDDESAL AAREDSGEHA PDASLEGVLA KLKAADGVST
     SEVTRVLDAA LVSPVFTAHP TETRRRTVFD VQKRIIKLLR ERHGILAQPQ TPRRITRLAE
     IEREAHLRMT ILWQTALIRI ARPQIEDEVN VGLRYFKRSL LEQVPAINRD TIAGLRDVFG
     GAVPNRQVVR TGSWIGGDHD GNPYVTGETL TYATRTAADT VLEYHVDQLG LLEKELSISD
     RYSESSAELQ ELAARGNNDV PSRVDEPYRR AIHGVLGRMT ATRASIAGDS VKDAAQDEVN
     EFAPYSSPAE FKAELDIIDR SLRQFNDAII ADDRLLRIRS ALDSFGFHLN ALDLRQNSES
     FEAVLDELFA GAGVTASGAG YKGLNEQAKR ELLAAELTSA RPLTFPWSAT YSEVTERELG
     IFRAAADAVD TLGVDVVPHC IVSMTGTVSD ILEPMVLLKE VGLLSFDPAR GRLVGSVDIA
     PLFETIDDLK AGAKILQELW DVPLYRDYLR GRGDTQEVVL GYSDSNKDGG YLSANWALYD
     AQLEIVEACN THGIGLRFSH GRGGAVGRGG GPTYDAILAQ PEGAVRGSVR ITEQGEVISA
     RYGTATTARR HLEAFVAGTL EASLLNTEKL KEPERAYSIM REISGLAGEK YASLVRHDEG
     FIDYFTQSTP LHEIGDLNMG SRPTARKQTE SIADLRAIPW VLSWSQSRVN LPGWFGVGTG
     ITRWAGDDDA RWDDLRTLYH AWPFFRSVLD NMAQVMGKAS MDLAKIYSTL VDDIETSQRV
     YNTIAEEYAL TREVFHRITD HDSLMAGNER LERSVQRRYP NLLPLNAIQI ELLRRYRAGD
     DSFLVSKTIQ VTMNGLATGL RTSG
//
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