GLMM_SHIFL
ID GLMM_SHIFL Reviewed; 445 AA.
AC Q83Q15;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Phosphoglucosamine mutase {ECO:0000255|HAMAP-Rule:MF_01554};
DE EC=5.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01554};
GN Name=glmM {ECO:0000255|HAMAP-Rule:MF_01554};
GN OrderedLocusNames=SF3216, S3434;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01554}.
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:0000255|HAMAP-Rule:MF_01554};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01554};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01554};
CC -!- PTM: Activated by phosphorylation. {ECO:0000255|HAMAP-Rule:MF_01554}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000255|HAMAP-Rule:MF_01554}.
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DR EMBL; AE005674; AAN44682.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18496.1; -; Genomic_DNA.
DR RefSeq; NP_708975.1; NC_004337.2.
DR AlphaFoldDB; Q83Q15; -.
DR SMR; Q83Q15; -.
DR STRING; 198214.SF3216; -.
DR EnsemblBacteria; AAN44682; AAN44682; SF3216.
DR EnsemblBacteria; AAP18496; AAP18496; S3434.
DR GeneID; 1024974; -.
DR KEGG; sfl:SF3216; -.
DR KEGG; sfx:S3434; -.
DR PATRIC; fig|198214.7.peg.3816; -.
DR HOGENOM; CLU_016950_7_0_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 3: Inferred from homology;
KW Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..445
FT /note="Phosphoglucosamine mutase"
FT /id="PRO_0000147955"
FT ACT_SITE 102
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT CONFLICT 258
FT /note="Y -> D (in Ref. 2; AAP18496)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="H -> Q (in Ref. 2; AAP18496)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="A -> D (in Ref. 2; AAP18496)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="T -> A (in Ref. 2; AAP18496)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="A -> E (in Ref. 2; AAP18496)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="T -> A (in Ref. 2; AAP18496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 47559 MW; 716CFB3B88B58489 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 DHEGNKVYGD QIMYIIAREG LRQGHLRGGA VGTLMSNMGL ELALKQLGIP
FARAKVGDRY VLEKMQEKGW RIGAENSGHV ILLDKTTTGA GIVAGLQVLT AMARNHMSLH
DLCSGMKMFP QILVNVRYTA GSGDPLEHES VKAVTAEVEA ALGNRGRVLL RKSGTEPLIR
VMVEGEDAAQ VTEFAHRITD AVKAV
