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
//