CAPP_ECOLI
ID CAPP_ECOLI Reviewed; 883 AA.
AC P00864; Q2M8Q1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Phosphoenolpyruvate carboxylase;
DE Short=PEPC;
DE Short=PEPCase;
DE EC=4.1.1.31;
GN Name=ppc; Synonyms=glu; OrderedLocusNames=b3956, JW3928;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6086598; DOI=10.1093/oxfordjournals.jbchem.a134718;
RA Fujita N., Miwa T., Ishijima S., Izui K., Katsuki H.;
RT "The primary structure of phosphoenolpyruvate carboxylase of Escherichia
RT coli. Nucleotide sequence of the ppc gene and deduced amino acid
RT sequence.";
RL J. Biochem. 95:909-916(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RC STRAIN=K12;
RX PubMed=1551850; DOI=10.1128/jb.174.7.2323-2331.1992;
RA Meinnel T., Schmitt E., Mechulam Y., Blanquet S.;
RT "Structural and biochemical characterization of the Escherichia coli argE
RT gene product.";
RL J. Bacteriol. 174:2323-2331(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
RX PubMed=3889833; DOI=10.1093/nar/13.1.59;
RA Izui K., Miwa T., Kajitani M., Fujita N., Sabe H., Ishihama I., Katsuki H.;
RT "Promoter analysis of the phosphoenolpyruvate carboxylase gene of
RT Escherichia coli.";
RL Nucleic Acids Res. 13:59-71(1985).
RN [7]
RP MUTAGENESIS OF HIS-579.
RX PubMed=2016273;
RA Terada K., Murata T., Izui K.;
RT "Site-directed mutagenesis of phosphoenolpyruvate carboxylase from E. coli:
RT the role of His579 in the catalytic and regulatory functions.";
RL J. Biochem. 109:49-54(1991).
RN [8]
RP MUTAGENESIS OF HIS-138.
RX PubMed=1765093; DOI=10.1111/j.1432-1033.1991.tb16435.x;
RA Terada K., Izui K.;
RT "Site-directed mutagenesis of the conserved histidine residue of
RT phosphoenolpyruvate carboxylase. His138 is essential for the second partial
RT reaction.";
RL Eur. J. Biochem. 202:797-803(1991).
RN [9]
RP MUTAGENESIS OF ARG-587.
RX PubMed=7490260; DOI=10.1093/oxfordjournals.jbchem.a124844;
RA Yano M., Terada K., Umiji K., Izui K.;
RT "Catalytic role of an arginine residue in the highly conserved and unique
RT sequence of phosphoenolpyruvate carboxylase.";
RL J. Biochem. 117:1196-1200(1995).
RN [10]
RP CRYSTALLIZATION.
RX PubMed=2677392; DOI=10.1016/0022-2836(89)90515-9;
RA Inoue M., Hayashi M., Sugimoto M., Harada S., Kai Y., Kasai N., Terada K.,
RA Izui K.;
RT "First crystallization of a phosphoenolpyruvate carboxylase from
RT Escherichia coli.";
RL J. Mol. Biol. 208:509-510(1989).
RN [11]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=9927652; DOI=10.1073/pnas.96.3.823;
RA Kai Y., Matsumura H., Inoue T., Terada K., Nagara Y., Yoshinaga T.,
RA Kihara A., Tsumura K., Izui K.;
RT "Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed
RT mechanism for allosteric inhibition.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:823-828(1999).
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: The enzyme has distinct binding sites for each of
CC the allosteric effectors such as acetyl-CoA, fructose 1,6-bisphosphate,
CC guanosine 3'-diphosphate 5'-diphosphate, long chain fatty acids, and L-
CC aspartate.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/PEPC/";
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DR EMBL; X05903; CAA29332.1; -; Genomic_DNA.
DR EMBL; X55417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00006; AAC43062.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76938.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77355.1; -; Genomic_DNA.
DR EMBL; X01700; CAA25847.1; -; Genomic_DNA.
DR PIR; A01083; QYEC.
DR RefSeq; NP_418391.1; NC_000913.3.
DR RefSeq; WP_001005586.1; NZ_SSZK01000014.1.
DR PDB; 1FIY; X-ray; 2.80 A; A=1-883.
DR PDB; 1JQN; X-ray; 2.35 A; A=1-883.
DR PDB; 1QB4; X-ray; 2.60 A; A=1-883.
DR PDBsum; 1FIY; -.
DR PDBsum; 1JQN; -.
DR PDBsum; 1QB4; -.
DR AlphaFoldDB; P00864; -.
DR SMR; P00864; -.
DR BioGRID; 4262649; 12.
DR DIP; DIP-10538N; -.
DR IntAct; P00864; 3.
DR STRING; 511145.b3956; -.
DR DrugBank; DB04317; 3,3-Dichloro-2-Phosphonomethyl-Acrylic Acid.
DR jPOST; P00864; -.
DR PaxDb; P00864; -.
DR PRIDE; P00864; -.
DR EnsemblBacteria; AAC76938; AAC76938; b3956.
DR EnsemblBacteria; BAE77355; BAE77355; BAE77355.
DR GeneID; 948457; -.
DR KEGG; ecj:JW3928; -.
DR KEGG; eco:b3956; -.
DR PATRIC; fig|1411691.4.peg.2749; -.
DR EchoBASE; EB0749; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_6; -.
DR InParanoid; P00864; -.
DR OMA; PWVFGWT; -.
DR PhylomeDB; P00864; -.
DR BioCyc; EcoCyc:PEPCARBOX-MON; -.
DR BioCyc; MetaCyc:PEPCARBOX-MON; -.
DR BRENDA; 4.1.1.31; 2026.
DR SABIO-RK; P00864; -.
DR EvolutionaryTrace; P00864; -.
DR PRO; PR:P00864; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:EcoCyc.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IMP:EcoCyc.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IMP:EcoCyc.
DR GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Carbon dioxide fixation; Lyase; Magnesium;
KW Reference proteome.
FT CHAIN 1..883
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166592"
FT ACT_SITE 138
FT ACT_SITE 546
FT /evidence="ECO:0000250"
FT MUTAGEN 138
FT /note="H->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1765093"
FT MUTAGEN 579
FT /note="H->N: 29% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:2016273"
FT MUTAGEN 579
FT /note="H->P: 5.4% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:2016273"
FT MUTAGEN 587
FT /note="R->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7490260"
FT HELIX 6..26
FT /evidence="ECO:0007829|PDB:1JQN"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 30..46
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 50..61
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 65..91
FT /evidence="ECO:0007829|PDB:1JQN"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:1JQN"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1JQN"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 168..187
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 213..231
FT /evidence="ECO:0007829|PDB:1JQN"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:1JQN"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 261..289
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:1JQN"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 311..334
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 349..365
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:1JQN"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:1JQN"
FT STRAND 390..398
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 399..412
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 423..435
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 449..463
FT /evidence="ECO:0007829|PDB:1JQN"
FT STRAND 468..475
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 480..491
FT /evidence="ECO:0007829|PDB:1JQN"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:1JQN"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 508..523
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 525..530
FT /evidence="ECO:0007829|PDB:1JQN"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:1JQN"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 541..548
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 550..571
FT /evidence="ECO:0007829|PDB:1JQN"
FT STRAND 574..579
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 589..597
FT /evidence="ECO:0007829|PDB:1JQN"
FT TURN 601..606
FT /evidence="ECO:0007829|PDB:1JQN"
FT STRAND 608..612
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 617..621
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 624..643
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 651..672
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 678..685
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 688..693
FT /evidence="ECO:0007829|PDB:1JQN"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:1QB4"
FT HELIX 709..711
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 714..723
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 728..730
FT /evidence="ECO:0007829|PDB:1JQN"
FT TURN 731..733
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 734..742
FT /evidence="ECO:0007829|PDB:1JQN"
FT TURN 743..745
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 747..756
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 758..773
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 776..786
FT /evidence="ECO:0007829|PDB:1JQN"
FT TURN 789..791
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 792..812
FT /evidence="ECO:0007829|PDB:1JQN"
FT TURN 818..821
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 823..856
FT /evidence="ECO:0007829|PDB:1JQN"
FT HELIX 862..879
FT /evidence="ECO:0007829|PDB:1JQN"
SQ SEQUENCE 883 AA; 99063 MW; 2620A776CF1F2EBC CRC64;
MNEQYSALRS NVSMLGKVLG ETIKDALGEH ILERVETIRK LSKSSRAGND ANRQELLTTL
QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPKGEAASN PEVIARTLRK LKNQPELSED
TIKKAVESLS LELVLTAHPT EITRRTLIHK MVEVNACLKQ LDNKDIADYE HNQLMRRLRQ
LIAQSWHTDE IRKLRPSPVD EAKWGFAVVE NSLWQGVPNY LRELNEQLEE NLGYKLPVEF
VPVRFTSWMG GDRDGNPNVT ADITRHVLLL SRWKATDLFL KDIQVLVSEL SMVEATPELL
ALVGEEGAAE PYRYLMKNLR SRLMATQAWL EARLKGEELP KPEGLLTQNE ELWEPLYACY
QSLQACGMGI IANGDLLDTL RRVKCFGVPL VRIDIRQEST RHTEALGELT RYLGIGDYES
WSEADKQAFL IRELNSKRPL LPRNWQPSAE TREVLDTCQV IAEAPQGSIA AYVISMAKTP
SDVLAVHLLL KEAGIGFAMP VAPLFETLDD LNNANDVMTQ LLNIDWYRGL IQGKQMVMIG
YSDSAKDAGV MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP
PGSLKGGLRV TEQGEMIRFK YGLPEITVSS LSLYTGAILE ANLLPPPEPK ESWRRIMDEL
SVISCDVYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA
WTQNRLMLPA WLGAGTALQK VVEDGKQSEL EAMCRDWPFF STRLGMLEMV FAKADLWLAE
YYDQRLVDKA LWPLGKELRN LQEEDIKVVL AIANDSHLMA DLPWIAESIQ LRNIYTDPLN
VLQAELLHRS RQAEKEGQEP DPRVEQALMV TIAGIAAGMR NTG
