GPMI_ECOLI
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 03-AUG-2022, entry version 165.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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_LN832404.1.
DR AlphaFoldDB; P37689; -.
DR SMR; P37689; -.
DR BioGRID; 4263294; 21.
DR DIP; DIP-12425N; -.
DR IntAct; P37689; 6.
DR STRING; 511145.b3612; -.
DR SWISS-2DPAGE; P37689; -.
DR jPOST; P37689; -.
DR PaxDb; P37689; -.
DR PRIDE; P37689; -.
DR EnsemblBacteria; AAC76636; AAC76636; b3612.
DR EnsemblBacteria; BAE77680; BAE77680; BAE77680.
DR GeneID; 948130; -.
DR KEGG; ecj:JW3587; -.
DR KEGG; eco:b3612; -.
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 PhylomeDB; P37689; -.
DR BioCyc; EcoCyc:PGMI-MON; -.
DR BioCyc; MetaCyc:PGMI-MON; -.
DR SABIO-RK; P37689; -.
DR UniPathway; UPA00109; UER00186.
DR PRO; PR:P37689; -.
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:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0044262; P:cellular 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 Gene3D; 3.40.1450.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR HAMAP; MF_01038; GpmI; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011258; BPG-indep_PGM_N.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR036646; PGAM_B_sf.
DR InterPro; IPR005995; Pgm_bpd_ind.
DR PANTHER; PTHR31637; PTHR31637; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001492; IPGAM; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF64158; SSF64158; 1.
DR TIGRFAMs; TIGR01307; pgm_bpd_ind; 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
