CAPP_CORCT
ID CAPP_CORCT Reviewed; 919 AA.
AC Q93MH3;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595};
OS Corynebacterium crenatum.
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=168810;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CD945;
RA Liu Y., Ding J., Wang Y.;
RT "Cloning and expression of phosphoenolpyruvate carboxylase-coding gene in
RT Corynebacterium crenatum CD945.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00595}.
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DR EMBL; AF406314; AAK92540.1; -; Genomic_DNA.
DR RefSeq; WP_006284539.1; NZ_JPDH01000002.1.
DR AlphaFoldDB; Q93MH3; -.
DR SMR; Q93MH3; -.
DR GeneID; 58309230; -.
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 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; PTHR30523; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation; Lyase; Magnesium.
FT CHAIN 1..919
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166588"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 579
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 919 AA; 103332 MW; 10AF3F464AFFE604 CRC64;
MTDFLRDDIR FLGRILGEVI AEQEGQEVYE LVEQARLTSF DIAKGNAEMD SLVQVFDGIT
PAKATPIARA FSHFALLANL AEDLHDEELR EQALDAGDTP PDSTLDATWL KLNEGNVGAE
AVADVLRNAE VAPVLTAHPT ETRRRTVFDA QKWITTHMRE RHALQSAEPT ARTQSKLDEI
EKNIRRRITI LWQTALIRVA RPRIEDEIEV GLRYYKLSLL EEIPRINRDV AVELRERFGE
DVPLKPVVKP GSWIGGDHDG NPYVTAGTVE YSTRRAAETV LKYYARQLHS LEHELSLSDR
MNEVTPQLLE LADAGHNDVP SRVDEPYRRA VHGVRGRILA TTAELIGEDA VEGVWFKVFT
PYASPEEFLN DALTIDHSLR ESNDVLIADD RLSVLISAIE SFGFNLYSLD LRQNSESYED
VLTELFERAQ VTANYRELSE EEKLEVLLKE LRSPRPLIPH GSDEYSEVTD RELGIFRTAS
EAVKKFGPRM VPHCIISMAS SVTDVLEPMV LLKEFGLIAA NGDNPRGTVD VIPLFETIED
LRAGAGILGE LWKIDLYRNY LLQRDNVQEV MLGYSDSNKD GGYFSANWAL YDAELQLVEL
CRSAGVKLRL FHGRGGTVGR GGGPSYDAIL AQPKGAVQGS VRITEQGEII SAKYGNPETA
RRNLEALVSA TLEASLLDVS ELTDHQRAYD IMSEISELSL KKYTSLVHED QGFIDYFTQS
TPLQEIGSLN IGSRPSSRKQ TSSVEDLRAI PWVLSWSQSR VMLPGWFGVG TALEQWIGEG
EQATQRIAEL QTLNESWPFF TSVLDNMAQV MSKAELRLAK LYADLIPDRE VAERVYSVIH
EEYFLTKKMF CVITGSDDLL DDNPLLARSV QRRYPYLLPL NVIQVEMMRR YRKGDQSEQV
SRNIQLTMNG LSTALRNSG