ID   GPMI_ECOLI              Reviewed;         514 AA.
AC   P37689; Q2M7S6;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-SEP-2026, entry version 179.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000303|PubMed:10437801};
DE            Short=BPG-independent PGAM {ECO:0000303|PubMed:10437801};
DE            Short=Phosphoglyceromutase {ECO:0000303|PubMed:10437801};
DE            Short=iPGM {ECO:0000303|PubMed:10437801};
DE            EC=5.4.2.12 {ECO:0000269|PubMed:10437801};
GN   Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; Synonyms=pgmI, yibO;
GN   OrderedLocusNames=b3612, JW3587;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
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   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=B / BL21;
RX   PubMed=10493123;
RX   DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA   Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT   "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT   chromatography.";
RL   Electrophoresis 20:2181-2195(1999).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP   ACTIVITY 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).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate (2-PGA)
CC       and 3-phosphoglycerate (3-PGA). {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=5.4.2.12; Evidence={ECO:0000269|PubMed:10437801};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:10437801};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:10437801};
CC   -!- ACTIVITY REGULATION: Insensitive to vanadate.
CC       {ECO:0000269|PubMed:10437801}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=210 uM for 3-PGA (at pH 7 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:10437801};
CC         KM=97 uM for 2-PGA (at pH 7 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:10437801};
CC         Note=kcat is 22 sec(-1) for mutase with 3-PGA as substrate (at pH 7
CC         and 30 degrees Celsius). kcat is 10 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:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10437801}.
CC   -!- DEVELOPMENTAL STAGE: Expressed most strongly in early exponential
CC       growth, with levels falling off as cells reached late log phase and
CC       stationary phase. {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 BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000305}.
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DR   EMBL; U00039; AAB18589.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76636.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77680.1; -; Genomic_DNA.
DR   PIR; S47833; S47833.
DR   RefSeq; NP_418069.1; NC_000913.3.
DR   RefSeq; WP_001350558.1; NZ_CP009789.1.
DR   AlphaFoldDB; P37689; -.
DR   SMR; P37689; -.
DR   BioGRID; 4263294; 23.
DR   DIP; DIP-12425N; -.
DR   FunCoup; P37689; 654.
DR   IntAct; P37689; 6.
DR   STRING; 511145.b3612; -.
DR   jPOST; P37689; -.
DR   PaxDb; 511145-b3612; -.
DR   EnsemblBacteria; AAC76636; AAC76636; b3612.
DR   GeneID; 948130; -.
DR   KEGG; ecj:JW3587; -.
DR   KEGG; eco:b3612; -.
DR   KEGG; ecoc:C3026_19585; -.
DR   PATRIC; fig|1411691.4.peg.3094; -.
DR   EchoBASE; EB2204; -.
DR   eggNOG; COG0696; Bacteria.
DR   HOGENOM; CLU_026099_2_0_6; -.
DR   InParanoid; P37689; -.
DR   OMA; FMDGRDT; -.
DR   OrthoDB; 9800863at2; -.
DR   PhylomeDB; P37689; -.
DR   BioCyc; EcoCyc:PGMI-MONOMER; -.
DR   BioCyc; MetaCyc:PGMI-MONOMER; -.
DR   BRENDA; 5.4.2.12; 2026.
DR   SABIO-RK; P37689; -.
DR   UniPathway; UPA00109; UER00186.
DR   PRO; PR:P37689; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IDA:EcoCyc.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR   CDD; cd16010; iPGM; 1.
DR   FunFam; 3.40.1450.10:FF:000001; 2,3-bisphosphoglycerate-independent phosphoglycerate mutase; 1.
DR   FunFam; 3.40.720.10:FF:000001; 2,3-bisphosphoglycerate-independent phosphoglycerate mutase; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 1.
DR   HAMAP; MF_01038; GpmI; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR011258; BPG-indep_PGM_core.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR036646; PGAM_B_sf.
DR   InterPro; IPR005995; Pgm_bpd_ind.
DR   NCBIfam; TIGR01307; pgm_bpd_ind; 1.
DR   NCBIfam; NF003897; PRK05434.1-5; 1.
DR   PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF06415; iPGM_N; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001492; IPGAM; 1.
DR   SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   1: Evidence at protein level;
KW   Glycolysis; Isomerase; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..514
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_0000212145"
FT   ACT_SITE        64
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         14
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         64
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         155..156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         263..266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         403
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         407
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         444
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         445
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         463
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
SQ   SEQUENCE   514 AA;  56194 MW;  BD4173C2BA2CEDD8 CRC64;
     MLVSKKPMVL VILDGYGYRE EQQDNAIFSA KTPVMDALWA NRPHTLIDAS GLEVGLPDRQ
     MGNSEVGHVN LGAGRIVYQD LTRLDVEIKD RAFFANPVLT GAVDKAKNAG KAVHIMGLLS
     AGGVHSHEDH IMAMVELAAE RGAEKIYLHA FLDGRDTPPR SAESSLKKFE EKFAALGKGR
     VASIIGRYYA MDRDNRWDRV EKAYDLLTLA QGEFQADTAV AGLQAAYARD ENDEFVKATV
     IRAEGQPDAA MEDGDALIFM NFRADRAREI TRAFVNADFD GFARKKVVNV DFVMLTEYAA
     DIKTAVAYPP ASLVNTFGEW MAKNDKTQLR ISETEKYAHV TFFFNGGVEE SFKGEDRILI
     NSPKVATYDL QPEMSSAELT EKLVAAIKSG KYDTIICNYP NGDMVGHTGV MEAAVKAVEA
     LDHCVEEVAK AVESVGGQLL ITADHGNAEQ MRDPATGQAH TAHTNLPVPL IYVGDKNVKA
     VEGGKLSDIA PTMLSLMGME IPQEMTGKPL FIVE
//