GPMB_ECOLI
ID GPMB_ECOLI Reviewed; 215 AA.
AC P0A7A2; P36942; Q2M5S2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable phosphoglycerate mutase GpmB {ECO:0000255|HAMAP-Rule:MF_01040};
DE EC=5.4.2.- {ECO:0000255|HAMAP-Rule:MF_01040};
DE AltName: Full=PGAM {ECO:0000255|HAMAP-Rule:MF_01040};
DE AltName: Full=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01040};
GN Name=gpmB {ECO:0000255|HAMAP-Rule:MF_01040}; Synonyms=ytjC;
GN OrderedLocusNames=b4395, JW4358;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8449900; DOI=10.1016/s0021-9258(18)53330-5;
RA Skarstad K., Thoeny B., Hwang D.S., Kornberg A.;
RT "A novel binding protein of the origin of the Escherichia coli
RT chromosome.";
RL J. Biol. Chem. 268:5365-5370(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01040};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01040}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. GpmB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01040}.
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DR EMBL; M97495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U14003; AAA97291.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77348.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78384.1; -; Genomic_DNA.
DR PIR; S56619; S56619.
DR RefSeq; NP_418812.1; NC_000913.3.
DR RefSeq; WP_000942344.1; NZ_STEB01000033.1.
DR AlphaFoldDB; P0A7A2; -.
DR SMR; P0A7A2; -.
DR BioGRID; 4261680; 6.
DR DIP; DIP-9829N; -.
DR IntAct; P0A7A2; 5.
DR STRING; 511145.b4395; -.
DR jPOST; P0A7A2; -.
DR PaxDb; P0A7A2; -.
DR PRIDE; P0A7A2; -.
DR EnsemblBacteria; AAC77348; AAC77348; b4395.
DR EnsemblBacteria; BAE78384; BAE78384; BAE78384.
DR GeneID; 66671717; -.
DR GeneID; 948918; -.
DR KEGG; ecj:JW4358; -.
DR KEGG; eco:b4395; -.
DR PATRIC; fig|1411691.4.peg.2289; -.
DR EchoBASE; EB2083; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_9_5_6; -.
DR InParanoid; P0A7A2; -.
DR OMA; TEWNVAR; -.
DR PhylomeDB; P0A7A2; -.
DR BioCyc; EcoCyc:PGAM2-MON; -.
DR UniPathway; UPA00109; UER00186.
DR PRO; PR:P0A7A2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01040; PGAM_GpmB; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR023086; Phosphoglycerate_mutase_GpmB.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..215
FT /note="Probable phosphoglycerate mutase GpmB"
FT /id="PRO_0000179946"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P62707, ECO:0000255|HAMAP-
FT Rule:MF_01040"
FT ACT_SITE 82
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62707, ECO:0000255|HAMAP-
FT Rule:MF_01040"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62707, ECO:0000255|HAMAP-
FT Rule:MF_01040"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62707, ECO:0000255|HAMAP-
FT Rule:MF_01040"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q3JWH7, ECO:0000255|HAMAP-
FT Rule:MF_01040"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q3JWH7, ECO:0000255|HAMAP-
FT Rule:MF_01040"
FT BINDING 82..85
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62707, ECO:0000255|HAMAP-
FT Rule:MF_01040"
FT BINDING 104..105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62707, ECO:0000255|HAMAP-
FT Rule:MF_01040"
FT BINDING 151..152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62707, ECO:0000255|HAMAP-
FT Rule:MF_01040"
FT SITE 150
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P62707, ECO:0000255|HAMAP-
FT Rule:MF_01040"
FT CONFLICT 148
FT /note="V -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 215 AA; 24065 MW; 3653DA0548B9E009 CRC64;
MLQVYLVRHG ETQWNAERRI QGQSDSPLTA KGEQQAMQVA TRAKELGITH IISSDLGRTR
RTAEIIAQAC GCDIIFDSRL RELNMGVLEK RHIDSLTEEE ENWRRQLVNG TVDGRIPEGE
SMQELSDRVN AALESCRDLP QGSRPLLVSH GIALGCLVST ILGLPAWAER RLRLRNCSIS
RVDYQESLWL ASGWVVETAG DISHLDAPAL DELQR
