PGK_ECOLI
ID PGK_ECOLI Reviewed; 387 AA.
AC P0A799; P11665; Q2M9R6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=b2926, JW2893;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / CS520;
RX PubMed=2546007; DOI=10.1111/j.1365-2958.1989.tb00221.x;
RA Alefounder P.R., Perham R.N.;
RT "Identification, molecular cloning and sequence analysis of a gene cluster
RT encoding the class II fructose 1,6-bisphosphate aldolase, 3-
RT phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate
RT dehydrogenase of Escherichia coli.";
RL Mol. Microbiol. 3:723-732(1989).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-24.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; X14436; CAA32604.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69093.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75963.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76990.1; -; Genomic_DNA.
DR PIR; S04733; TVECG.
DR RefSeq; NP_417401.1; NC_000913.3.
DR RefSeq; WP_000111269.1; NZ_STEB01000001.1.
DR PDB; 1ZMR; X-ray; 2.40 A; A=1-387.
DR PDBsum; 1ZMR; -.
DR AlphaFoldDB; P0A799; -.
DR SMR; P0A799; -.
DR BioGRID; 4262834; 42.
DR BioGRID; 851735; 1.
DR DIP; DIP-36163N; -.
DR IntAct; P0A799; 16.
DR STRING; 511145.b2926; -.
DR iPTMnet; P0A799; -.
DR SWISS-2DPAGE; P0A799; -.
DR jPOST; P0A799; -.
DR PaxDb; P0A799; -.
DR PRIDE; P0A799; -.
DR EnsemblBacteria; AAC75963; AAC75963; b2926.
DR EnsemblBacteria; BAE76990; BAE76990; BAE76990.
DR GeneID; 67415187; -.
DR GeneID; 947414; -.
DR KEGG; ecj:JW2893; -.
DR KEGG; eco:b2926; -.
DR PATRIC; fig|1411691.4.peg.3806; -.
DR EchoBASE; EB0697; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_6; -.
DR InParanoid; P0A799; -.
DR OMA; DMIFDIG; -.
DR PhylomeDB; P0A799; -.
DR BioCyc; EcoCyc:PGK; -.
DR BioCyc; MetaCyc:PGK; -.
DR BRENDA; 2.7.2.3; 2026.
DR SABIO-RK; P0A799; -.
DR UniPathway; UPA00109; UER00185.
DR EvolutionaryTrace; P0A799; -.
DR PRO; PR:P0A799; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IDA:EcoCyc.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IDA:EcoCyc.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 2.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9600841, ECO:0000269|Ref.5"
FT CHAIN 2..387
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145941"
FT BINDING 21..23
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 59..62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 340..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 84
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1ZMR"
FT TURN 116..121
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1ZMR"
FT TURN 149..153
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 182..192
FT /evidence="ECO:0007829|PDB:1ZMR"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 255..266
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 341..350
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1ZMR"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 364..370
FT /evidence="ECO:0007829|PDB:1ZMR"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:1ZMR"
SQ SEQUENCE 387 AA; 41118 MW; FAD7D66D100514B2 CRC64;
MSVIKMTDLD LAGKRVFIRA DLNVPVKDGK VTSDARIRAS LPTIELALKQ GAKVMVTSHL
GRPTEGEYNE EFSLLPVVNY LKDKLSNPVR LVKDYLDGVD VAEGELVVLE NVRFNKGEKK
DDETLSKKYA ALCDVFVMDA FGTAHRAQAS THGIGKFADV ACAGPLLAAE LDALGKALKE
PARPMVAIVG GSKVSTKLTV LDSLSKIADQ LIVGGGIANT FIAAQGHDVG KSLYEADLVD
EAKRLLTTCN IPVPSDVRVA TEFSETAPAT LKSVNDVKAD EQILDIGDAS AQELAEILKN
AKTILWNGPV GVFEFPNFRK GTEIVANAIA DSEAFSIAGG GDTLAAIDLF GIADKISYIS
TGGGAFLEFV EGKVLPAVAM LEERAKK
