ID GPMA_ECOLI Reviewed; 250 AA.
AC P62707; P31217;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 24-JAN-2024, entry version 154.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000303|PubMed:10437801};
DE Short=BPG-dependent PGAM {ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000303|PubMed:10437801};
DE Short=PGAM {ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000303|PubMed:10437801};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000303|PubMed:10437801};
DE Short=dPGM {ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000303|PubMed:10437801};
DE EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000269|PubMed:10437801};
GN Name=gpmA {ECO:0000255|HAMAP-Rule:MF_01039}; Synonyms=gpm, pgm, pgmA;
GN OrderedLocusNames=b0755, JW0738;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Bouffard G.G., Ogihara N., Rudd K.E., Adhya S.L.;
RL Unpublished observations (MAY-1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-250.
RC STRAIN=K12;
RX PubMed=6125934; DOI=10.1093/nar/10.13.4045;
RA Davies W.D., Davidson B.E.;
RT "The nucleotide sequence of aroG, the gene for 3-deoxy-D-
RT arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli
RT K12.";
RL Nucleic Acids Res. 10:4045-4058(1982).
RN [6]
RP PROTEIN SEQUENCE OF 2-20.
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 [7]
RP PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 2-11.
RX PubMed=8670822; DOI=10.1002/j.1460-2075.1996.tb00686.x;
RA Nystroem T., Larsson C., Gustafsson L.;
RT "Bacterial defense against aging: role of the Escherichia coli ArcA
RT regulator in gene expression, readjusted energy flux and survival during
RT stasis.";
RL EMBO J. 15:3219-3228(1996).
RN [9]
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 [10]
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, DEVELOPMENTAL STAGE, AND SUBUNIT.
RX PubMed=10437801; DOI=10.1016/s0014-5793(99)00910-2;
RA Fraser H.I., Kvaratskhelia M., White M.F.;
RT "The two analogous phosphoglycerate mutases of Escherichia coli.";
RL FEBS Lett. 455:344-348(1999).
RN [12]
RP INDUCTION.
RX PubMed=11101675; DOI=10.1099/00221287-146-12-3171;
RA Vassinova N., Kozyrev D.;
RT "A method for direct cloning of Fur-regulated genes: identification of
RT seven new Fur-regulated loci in Escherichia coli.";
RL Microbiology 146:3171-3182(2000).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-100 AND LYS-106, AND
RP IDENTIFICATION BY MASS 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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP ACTIVE SITE, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=11038361; DOI=10.1074/jbc.m007318200;
RA Bond C.S., White M.F., Hunter W.N.;
RT "High resolution structure of the phosphohistidine-activated form of
RT Escherichia coli cofactor-dependent phosphoglycerate mutase.";
RL J. Biol. Chem. 276:3247-3253(2001).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH VANADATE, SUBUNIT,
RP AND ACTIVE SITE.
RX PubMed=11884145; DOI=10.1006/jmbi.2002.5418;
RA Bond C.S., White M.F., Hunter W.N.;
RT "Mechanistic implications for Escherichia coli cofactor-dependent
RT phosphoglycerate mutase based on the high-resolution crystal structure of a
RT vanadate complex.";
RL J. Mol. Biol. 316:1071-1081(2002).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039,
CC ECO:0000269|PubMed:10437801}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01039,
CC ECO:0000269|PubMed:10437801};
CC -!- ACTIVITY REGULATION: Strongly inhibited by vanadate.
CC {ECO:0000269|PubMed:10437801}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=190 uM for 2-PGA (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10437801};
CC KM=200 uM for 3-PGA (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10437801};
CC Note=kcat is 330 sec(-1) for mutase with 3-PGA as substrate (at pH 7
CC and 30 degrees Celsius). kcat is 220 sec(-1) for mutase with 2-PGA as
CC substrate (at pH 7 and 30 degrees Celsius).
CC {ECO:0000269|PubMed:10437801};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01039}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01039,
CC ECO:0000269|PubMed:10437801, ECO:0000269|PubMed:11038361,
CC ECO:0000269|PubMed:11884145}.
CC -!- DEVELOPMENTAL STAGE: Peak expression observed in mid to late log phase.
CC {ECO:0000269|PubMed:10437801}.
CC -!- INDUCTION: Regulated by the Fur protein. {ECO:0000269|PubMed:11101675}.
CC -!- MISCELLANEOUS: Has a 10-fold higher specific activity than BPG-
CC independent phosphoglycerate mutase. {ECO:0000269|PubMed:10437801}.
CC -!- MISCELLANEOUS: Inhibition by vanadate is a diagnostic test for
CC discrimination between the cofactor-dependent (GpmA) and -independent
CC (GpmI) phosphoglycerate mutases. {ECO:0000269|PubMed:10437801}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}.
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DR EMBL; U00096; AAC73842.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35417.1; -; Genomic_DNA.
DR EMBL; J01591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C64811; C64811.
DR RefSeq; NP_415276.1; NC_000913.3.
DR RefSeq; WP_001295305.1; NZ_STEB01000028.1.
DR PDB; 1E58; X-ray; 1.25 A; A=2-250.
DR PDB; 1E59; X-ray; 1.30 A; A=2-250.
DR PDBsum; 1E58; -.
DR PDBsum; 1E59; -.
DR AlphaFoldDB; P62707; -.
DR SMR; P62707; -.
DR BioGRID; 4259673; 8.
DR DIP; DIP-35899N; -.
DR IntAct; P62707; 16.
DR STRING; 511145.b0755; -.
DR iPTMnet; P62707; -.
DR SWISS-2DPAGE; P62707; -.
DR jPOST; P62707; -.
DR PaxDb; 511145-b0755; -.
DR EnsemblBacteria; AAC73842; AAC73842; b0755.
DR GeneID; 83577323; -.
DR GeneID; 945068; -.
DR KEGG; ecj:JW0738; -.
DR KEGG; eco:b0755; -.
DR PATRIC; fig|1411691.4.peg.1524; -.
DR EchoBASE; EB1650; -.
DR eggNOG; COG0588; Bacteria.
DR HOGENOM; CLU_033323_1_1_6; -.
DR InParanoid; P62707; -.
DR OMA; RMLPYWY; -.
DR OrthoDB; 9781415at2; -.
DR PhylomeDB; P62707; -.
DR BioCyc; EcoCyc:GPMA-MONOMER; -.
DR BioCyc; MetaCyc:GPMA-MONOMER; -.
DR SABIO-RK; P62707; -.
DR UniPathway; UPA00109; UER00186.
DR EvolutionaryTrace; P62707; -.
DR PRO; PR:P62707; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR GO; GO:0061621; P:canonical glycolysis; IGI:EcoCyc.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR NCBIfam; TIGR01258; pgm_1; 1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Gluconeogenesis;
KW Glycolysis; Isomerase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8670822,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9600841,
FT ECO:0000269|Ref.7"
FT CHAIN 2..250
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_0000179873"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:11038361, ECO:0000269|PubMed:11884145"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:11038361, ECO:0000269|PubMed:11884145"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:11884145"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:11038361, ECO:0000269|PubMed:11884145"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q3JWH7, ECO:0000255|HAMAP-
FT Rule:MF_01039"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:11884145"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:11884145"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:11038361, ECO:0000269|PubMed:11884145"
FT BINDING 185..186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:11884145"
FT SITE 184
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:11038361"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 32..47
FT /evidence="ECO:0007829|PDB:1E58"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:1E58"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1E58"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 154..167
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:1E58"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:1E58"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1E58"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1E58"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:1E58"
SQ SEQUENCE 250 AA; 28556 MW; A6E0A49406F8482A CRC64;
MAVTKLVLVR HGESQWNKEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGY SFDFAYTSVL
KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK AETAEKYGDE QVKQWRRGFA
VTPPELTKDD ERYPGHDPRY AKLSEKELPL TESLALTIDR VIPYWNETIL PRMKSGERVI
IAAHGNSLRA LVKYLDNMSE EEILELNIPT GVPLVYEFDE NFKPLKRYYL GNADEIAAKA
AAVANQGKAK
//
