GLMM_STAAC
ID GLMM_STAAC Reviewed; 451 AA.
AC Q5HE43; P95685; P95710;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Phosphoglucosamine mutase;
DE EC=5.4.2.10;
GN Name=glmM; Synonyms=femD; OrderedLocusNames=SACOL2151;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=COL;
RX PubMed=9158773; DOI=10.1089/mdr.1996.2.277;
RA Wu S., de Lencastre H., Sali A., Tomasz A.;
RT "A phosphoglucomutase-like gene essential for the optimal expression of
RT methicillin resistance in Staphylococcus aureus: molecular cloning and DNA
RT sequencing.";
RL Microb. Drug Resist. 2:277-286(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9286983; DOI=10.1128/jb.179.17.5321-5325.1997;
RA Jolly L., Wu S.W., Van Heijenoort J., de Lencastre H., Mengin-Lecreulx D.,
RA Tomasz A.;
RT "The femR315 gene from Staphylococcus aureus, the interruption of which
RT results in reduced methicillin resistance, encodes a phosphoglucosamine
RT mutase.";
RL J. Bacteriol. 179:5321-5325(1997).
RN [4]
RP PHOSPHORYLATION AT SER-102.
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. {ECO:0000269|PubMed:9286983}.
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:9286983};
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 -!- PTM: Activated by phosphorylation. Can autophosphorylate in vitro using
CC ATP. {ECO:0000269|PubMed:10671448}.
CC -!- DISRUPTION PHENOTYPE: Disruption results in a drastically reduced
CC methicillin resistance. {ECO:0000269|PubMed:9158773}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; Y09927; CAA71060.2; -; Genomic_DNA.
DR EMBL; CP000046; AAW38459.1; -; Genomic_DNA.
DR RefSeq; WP_000521491.1; NC_002951.2.
DR AlphaFoldDB; Q5HE43; -.
DR SMR; Q5HE43; -.
DR iPTMnet; Q5HE43; -.
DR EnsemblBacteria; AAW38459; AAW38459; SACOL2151.
DR KEGG; sac:SACOL2151; -.
DR HOGENOM; CLU_016950_7_0_9; -.
DR OMA; PHNPEPL; -.
DR Proteomes; UP000000530; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 Isomerase; Magnesium; Metal-binding; Phosphoprotein.
FT CHAIN 1..451
FT /note="Phosphoglucosamine mutase"
FT /id="PRO_0000147959"
FT ACT_SITE 102
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 246
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:0000305|PubMed:10671448"
SQ SEQUENCE 451 AA; 49266 MW; A164B280C4B9ABD8 CRC64;
MGKYFGTDGV RGVANQELTP ELAFKLGRYG GYVLAHNKGE KHPRVLVGRD TRVSGEMLES
ALIAGLISIG AEVMRLGIIS TPGVAYLTRD MGAELGVMIS ASHNPVADNG IKFFGSDGFK
LSDEQENEIE ALLDQENPEL PRPVGNDIVH YSDYFEGAQK YLSYLKSTVD VNFEGLKIAL
DGANGSTSSL APFLFGDLEA DTETIGCSPD GYNINEKCGS THPEKLAEKV VETESDFGLA
FDGDGDRIIA VDENGQIVDG DQIMFIIGQE MHKNQELNND MIVSTVMSNL GFYKALEQEG
IKSNKTKVGD RYVVEEMRRG NYNLGGEQSG HIVMMDYNTT GDGLLTGIQL ASVIKMTGKS
LSELAGQMKK YPQSLINVRV TDKYRVEENV DVKEVMTKVE VEMNGEGRIL VRPSGTEPLV
RVMVEAATDE DAERFAQQIA DVVQDKMGLD K
