GLMM_ECOLI
ID GLMM_ECOLI Reviewed; 445 AA.
AC P31120; Q2M936;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Phosphoglucosamine mutase;
DE EC=5.4.2.10 {ECO:0000269|PubMed:10231382};
GN Name=glmM; Synonyms=mrsA, yhbF; OrderedLocusNames=b3176, JW3143;
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=8244950; DOI=10.1128/jb.175.23.7743-7744.1993;
RA Dallas W.S., Dev I.K., Ray P.H.;
RT "The dihydropteroate synthase gene, folP, is near the leucine tRNA gene,
RT leuU, on the Escherichia coli chromosome.";
RL J. Bacteriol. 175:7743-7744(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Wang R., Kushner S.R.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
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 PROTEIN SEQUENCE OF 2-12, AND CHARACTERIZATION.
RX PubMed=8550580; DOI=10.1074/jbc.271.1.32;
RA Mengin-Lecreulx D., van Heijenoort J.;
RT "Characterization of the essential gene glmM encoding phosphoglucosamine
RT mutase in Escherichia coli.";
RL J. Biol. Chem. 271:32-39(1996).
RN [6]
RP PHOSPHORYLATION AT SER-102, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-100 AND
RP SER-102.
RX PubMed=10231382; DOI=10.1046/j.1432-1327.1999.00373.x;
RA Jolly L., Ferrari P., Blanot D., Van Heijenoort J., Fassy F.,
RA Mengin-Lecreulx D.;
RT "Reaction mechanism of phosphoglucosamine mutase from Escherichia coli.";
RL Eur. J. Biochem. 262:202-210(1999).
RN [7]
RP PHOSPHORYLATION AT SER-102, KINETIC PARAMETERS, ACTIVITY REGULATION, AND
RP ACTIVE SITE.
RX PubMed=10671448; DOI=10.1128/jb.182.5.1280-1285.2000;
RA Jolly L., Pompeo F., van Heijenoort J., Fassy F., Mengin-Lecreulx D.;
RT "Autophosphorylation of phosphoglucosamine mutase from Escherichia coli.";
RL J. Bacteriol. 182:1280-1285(2000).
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. Can also catalyze the formation of glucose-6-P
CC from glucose-1-P, although at a 1400-fold lower rate.
CC {ECO:0000269|PubMed:10231382}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate;
CC Xref=Rhea:RHEA:23424, ChEBI:CHEBI:58516, ChEBI:CHEBI:58725;
CC EC=5.4.2.10; Evidence={ECO:0000269|PubMed:10231382};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23425;
CC Evidence={ECO:0000269|PubMed:10231382};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23426;
CC Evidence={ECO:0000269|PubMed:10231382};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Autophosphorylation is inhibited by inorganic
CC phosphate or EDTA. {ECO:0000269|PubMed:10671448}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.05 mM for glucosamine-6-P {ECO:0000269|PubMed:10231382,
CC ECO:0000269|PubMed:10671448};
CC KM=0.08 mM for glucosamine-1,6-diP {ECO:0000269|PubMed:10231382,
CC ECO:0000269|PubMed:10671448};
CC KM=0.5 mM for glucose-1,6-diP {ECO:0000269|PubMed:10231382,
CC ECO:0000269|PubMed:10671448};
CC KM=0.65 mM for glucose-1-P {ECO:0000269|PubMed:10231382,
CC ECO:0000269|PubMed:10671448};
CC KM=0.06 mM for ATP {ECO:0000269|PubMed:10231382,
CC ECO:0000269|PubMed:10671448};
CC -!- PTM: Activated by phosphorylation. Can autophosphorylate in vitro using
CC ATP, alpha-D-glucosamine 1,6-bisphosphate or alpha-D-glucose 1,6-
CC bisphosphate. {ECO:0000269|PubMed:10231382,
CC ECO:0000269|PubMed:10671448}.
CC -!- MISCELLANEOUS: Catalysis proceeds by a classical ping-pong bi-bi
CC reaction mechanism, with alpha-D-glucosamine 1,6-bisphosphate as an
CC intermediate.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; L12968; AAA16122.1; -; Unassigned_DNA.
DR EMBL; U01376; AAA97510.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57977.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76208.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77220.1; -; Genomic_DNA.
DR PIR; I41215; I41215.
DR RefSeq; NP_417643.1; NC_000913.3.
DR RefSeq; WP_000071134.1; NZ_STEB01000012.1.
DR AlphaFoldDB; P31120; -.
DR SMR; P31120; -.
DR BioGRID; 4263256; 227.
DR DIP; DIP-10260N; -.
DR IntAct; P31120; 16.
DR STRING; 511145.b3176; -.
DR iPTMnet; P31120; -.
DR jPOST; P31120; -.
DR PaxDb; P31120; -.
DR PRIDE; P31120; -.
DR EnsemblBacteria; AAC76208; AAC76208; b3176.
DR EnsemblBacteria; BAE77220; BAE77220; BAE77220.
DR GeneID; 66672922; -.
DR GeneID; 947692; -.
DR KEGG; ecj:JW3143; -.
DR KEGG; eco:b3176; -.
DR PATRIC; fig|1411691.4.peg.3556; -.
DR EchoBASE; EB1514; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_0_6; -.
DR InParanoid; P31120; -.
DR OMA; PHNPEPL; -.
DR PhylomeDB; P31120; -.
DR BioCyc; EcoCyc:PHOSGLUCOSAMINEMUT-MON; -.
DR BioCyc; MetaCyc:PHOSGLUCOSAMINEMUT-MON; -.
DR SABIO-RK; P31120; -.
DR PRO; PR:P31120; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IDA:EcoCyc.
DR GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:EcoCyc.
DR CDD; cd05802; GlmM; 1.
DR HAMAP; MF_01554_B; GlmM_B; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR006352; GlmM_bact.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR TIGRFAMs; TIGR01455; glmM; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Isomerase; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8550580"
FT CHAIN 2..445
FT /note="Phosphoglucosamine mutase"
FT /id="PRO_0000147887"
FT ACT_SITE 102
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000269|PubMed:10671448"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 102
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10231382,
FT ECO:0000269|PubMed:10671448"
FT MUTAGEN 100
FT /note="S->A: 2% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10231382"
FT MUTAGEN 100
FT /note="S->T: 20-fold increase in the non-specific
FT phosphoglucomutase activity towards glucose-phosphate
FT substrates (non aminated)."
FT /evidence="ECO:0000269|PubMed:10231382"
FT MUTAGEN 102
FT /note="S->A: Loss of activity in the absence or presence of
FT glucosamine-1,6-diP."
FT /evidence="ECO:0000269|PubMed:10231382"
FT CONFLICT 69
FT /note="A -> R (in Ref. 2; AAA97510)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="C -> S (in Ref. 2; AAA97510)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="P -> R (in Ref. 2; AAA97510)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..181
FT /note="VVDC -> LVIG (in Ref. 2; AAA97510)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="R -> C (in Ref. 2; AAA97510)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="P -> R (in Ref. 2; AAA97510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 47544 MW; ECDF9A0378A980EC CRC64;
MSNRKYFGTD GIRGRVGDAP ITPDFVLKLG WAAGKVLARH GSRKIIIGKD TRISGYMLES
ALEAGLAAAG LSALFTGPMP TPAVAYLTRT FRAEAGIVIS ASHNPFYDNG IKFFSIDGTK
LPDAVEEAIE AEMEKEISCV DSAELGKASR IVDAAGRYIE FCKATFPNEL SLSELKIVVD
CANGATYHIA PNVLRELGAN VIAIGCEPNG VNINAEVGAT DVRALQARVL AEKADLGIAF
DGDGDRVIMV DHEGNKVDGD QIMYIIAREG LRQGQLRGGA VGTLMSNMGL ELALKQLGIP
FARAKVGDRY VLEKMQEKGW RIGAENSGHV ILLDKTTTGD GIVAGLQVLA AMARNHMSLH
DLCSGMKMFP QILVNVRYTA GSGDPLEHES VKAVTAEVEA ALGNRGRVLL RKSGTEPLIR
VMVEGEDEAQ VTEFAHRIAD AVKAV
