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Database: UniProt/SWISS-PROT
Entry: CAPP_ECOLI
LinkDB: CAPP_ECOLI
Original site: 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   22-NOV-2017, entry version 160.
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;
RA   Fujita N., Miwa T., Ishijima S., Izui K., Katsuki H.;
RT   "The primary structure of phosphoenolpyruvate carboxylase of
RT   Escherichia coli. Nucleotide sequence of the ppc gene and deduced
RT   amino acid 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.,
RA   Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the
RT   region 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.,
RA   Mau B., 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
RT   MG1655 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
RT   argE 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.,
RA   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.
RT   coli: 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
RT   partial reaction.";
RL   Eur. J. Biochem. 202:797-803(1991).
RN   [9]
RP   MUTAGENESIS OF ARG-587.
RX   PubMed=7490260;
RA   Yano M., Terada K., Umiji K., Izui K.;
RT   "Catalytic role of an arginine residue in the highly conserved and
RT   unique 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.,
RA   Terada K., 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.,
RA   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
RT   proposed 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
CC       source for the tricarboxylic acid cycle.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ENZYME REGULATION: The enzyme has distinct binding sites for each
CC       of the allosteric effectors such as acetyl-CoA, fructose 1,6-
CC       bisphosphate, guanosine 3'-diphosphate 5'-diphosphate, long chain
CC       fatty acids, and L-aspartate.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="http://www.worthington-biochem.com/PEPC/";
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_LN832404.1.
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   ProteinModelPortal; P00864; -.
DR   SMR; P00864; -.
DR   BioGrid; 4262649; 8.
DR   DIP; DIP-10538N; -.
DR   IntAct; P00864; 3.
DR   STRING; 316385.ECDH10B_4144; -.
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   EcoGene; EG10756; ppc.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   InParanoid; P00864; -.
DR   KO; K01595; -.
DR   PhylomeDB; P00864; -.
DR   BioCyc; EcoCyc:PEPCARBOX-MONOMER; -.
DR   BioCyc; MetaCyc:PEPCARBOX-MONOMER; -.
DR   BRENDA; 4.1.1.31; 2026.
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:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:EcoCyc.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
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;
KW   Complete proteome; Lyase; Magnesium; Reference proteome.
FT   CHAIN         1    883       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000166592.
FT   ACT_SITE    138    138
FT   ACT_SITE    546    546       {ECO:0000250}.
FT   MUTAGEN     138    138       H->N: Loss of activity.
FT                                {ECO:0000269|PubMed:1765093}.
FT   MUTAGEN     579    579       H->N: 29% of wild-type activity.
FT                                {ECO:0000269|PubMed:2016273}.
FT   MUTAGEN     579    579       H->P: 5.4% of wild-type activity.
FT                                {ECO:0000269|PubMed:2016273}.
FT   MUTAGEN     587    587       R->S: Loss of activity.
FT                                {ECO:0000269|PubMed:7490260}.
FT   HELIX         6     26       {ECO:0000244|PDB:1JQN}.
FT   TURN         27     29       {ECO:0000244|PDB:1JQN}.
FT   HELIX        30     46       {ECO:0000244|PDB:1JQN}.
FT   HELIX        50     61       {ECO:0000244|PDB:1JQN}.
FT   HELIX        65     91       {ECO:0000244|PDB:1JQN}.
FT   TURN         93     96       {ECO:0000244|PDB:1JQN}.
FT   HELIX       102    112       {ECO:0000244|PDB:1JQN}.
FT   HELIX       119    127       {ECO:0000244|PDB:1JQN}.
FT   STRAND      131    135       {ECO:0000244|PDB:1JQN}.
FT   STRAND      143    145       {ECO:0000244|PDB:1JQN}.
FT   HELIX       148    161       {ECO:0000244|PDB:1JQN}.
FT   HELIX       168    187       {ECO:0000244|PDB:1JQN}.
FT   HELIX       198    211       {ECO:0000244|PDB:1JQN}.
FT   HELIX       213    231       {ECO:0000244|PDB:1JQN}.
FT   STRAND      243    247       {ECO:0000244|PDB:1JQN}.
FT   TURN        249    251       {ECO:0000244|PDB:1JQN}.
FT   HELIX       261    289       {ECO:0000244|PDB:1JQN}.
FT   HELIX       297    303       {ECO:0000244|PDB:1JQN}.
FT   STRAND      307    310       {ECO:0000244|PDB:1JQN}.
FT   HELIX       311    334       {ECO:0000244|PDB:1JQN}.
FT   HELIX       349    365       {ECO:0000244|PDB:1JQN}.
FT   HELIX       369    372       {ECO:0000244|PDB:1JQN}.
FT   HELIX       375    385       {ECO:0000244|PDB:1JQN}.
FT   TURN        386    389       {ECO:0000244|PDB:1JQN}.
FT   STRAND      390    398       {ECO:0000244|PDB:1JQN}.
FT   HELIX       399    412       {ECO:0000244|PDB:1JQN}.
FT   HELIX       418    420       {ECO:0000244|PDB:1JQN}.
FT   HELIX       423    435       {ECO:0000244|PDB:1JQN}.
FT   HELIX       449    463       {ECO:0000244|PDB:1JQN}.
FT   STRAND      468    475       {ECO:0000244|PDB:1JQN}.
FT   HELIX       480    491       {ECO:0000244|PDB:1JQN}.
FT   TURN        492    494       {ECO:0000244|PDB:1JQN}.
FT   STRAND      501    505       {ECO:0000244|PDB:1JQN}.
FT   HELIX       508    523       {ECO:0000244|PDB:1JQN}.
FT   HELIX       525    530       {ECO:0000244|PDB:1JQN}.
FT   TURN        531    533       {ECO:0000244|PDB:1JQN}.
FT   STRAND      534    539       {ECO:0000244|PDB:1JQN}.
FT   HELIX       541    548       {ECO:0000244|PDB:1JQN}.
FT   HELIX       550    571       {ECO:0000244|PDB:1JQN}.
FT   STRAND      574    579       {ECO:0000244|PDB:1JQN}.
FT   HELIX       584    586       {ECO:0000244|PDB:1JQN}.
FT   HELIX       589    597       {ECO:0000244|PDB:1JQN}.
FT   TURN        601    606       {ECO:0000244|PDB:1JQN}.
FT   STRAND      608    612       {ECO:0000244|PDB:1JQN}.
FT   HELIX       614    616       {ECO:0000244|PDB:1JQN}.
FT   HELIX       617    621       {ECO:0000244|PDB:1JQN}.
FT   HELIX       624    643       {ECO:0000244|PDB:1JQN}.
FT   HELIX       651    672       {ECO:0000244|PDB:1JQN}.
FT   HELIX       678    685       {ECO:0000244|PDB:1JQN}.
FT   HELIX       688    693       {ECO:0000244|PDB:1JQN}.
FT   STRAND      697    699       {ECO:0000244|PDB:1QB4}.
FT   HELIX       709    711       {ECO:0000244|PDB:1JQN}.
FT   HELIX       714    723       {ECO:0000244|PDB:1JQN}.
FT   HELIX       728    730       {ECO:0000244|PDB:1JQN}.
FT   TURN        731    733       {ECO:0000244|PDB:1JQN}.
FT   HELIX       734    742       {ECO:0000244|PDB:1JQN}.
FT   TURN        743    745       {ECO:0000244|PDB:1JQN}.
FT   HELIX       747    756       {ECO:0000244|PDB:1JQN}.
FT   HELIX       758    773       {ECO:0000244|PDB:1JQN}.
FT   HELIX       776    786       {ECO:0000244|PDB:1JQN}.
FT   TURN        789    791       {ECO:0000244|PDB:1JQN}.
FT   HELIX       792    812       {ECO:0000244|PDB:1JQN}.
FT   TURN        818    821       {ECO:0000244|PDB:1JQN}.
FT   HELIX       823    856       {ECO:0000244|PDB:1JQN}.
FT   HELIX       862    879       {ECO:0000244|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
//
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