GLMM_FRATT
ID GLMM_FRATT Reviewed; 443 AA.
AC Q5NII8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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}; OrderedLocusNames=FTT_0079;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG44712.1; -; Genomic_DNA.
DR RefSeq; WP_003019799.1; NZ_CP010290.1.
DR RefSeq; YP_169154.1; NC_006570.2.
DR PDB; 3I3W; X-ray; 2.30 A; A/B=1-443.
DR PDBsum; 3I3W; -.
DR AlphaFoldDB; Q5NII8; -.
DR SMR; Q5NII8; -.
DR STRING; 177416.FTT_0079; -.
DR DNASU; 3191618; -.
DR EnsemblBacteria; CAG44712; CAG44712; FTT_0079.
DR KEGG; ftu:FTT_0079; -.
DR eggNOG; COG1109; Bacteria.
DR OMA; VDCGNGM; -.
DR EvolutionaryTrace; Q5NII8; -.
DR Proteomes; UP000001174; 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..443
FT /note="Phosphoglucosamine mutase"
FT /id="PRO_0000147890"
FT ACT_SITE 101
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 101
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 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT STRAND 7..20
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 21..37
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3I3W"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:3I3W"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3I3W"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:3I3W"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:3I3W"
FT TURN 267..272
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:3I3W"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:3I3W"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 388..398
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:3I3W"
FT STRAND 412..423
FT /evidence="ECO:0007829|PDB:3I3W"
FT HELIX 424..441
FT /evidence="ECO:0007829|PDB:3I3W"
SQ SEQUENCE 443 AA; 48185 MW; 8EE0B69868BDEECE CRC64;
MAKYFGTDGI RGEVANSTIT VEFTQKLGNA VGSLINQKNY PKFVIVGQDT RSSGGFLKFA
LVSGLNAAGI DVLDLGVVPT PVVAFMTVKH RAAAGFVITA SHNKFTDNGI KLFSSNGFKL
DDALEEEVED MIDGDFIYQP QFKFGSYKIL ANAIDEYIES IYSRFAKFVN YKGKVVVDCA
HGAASHNFEA LLDKFGINYV SIASNPDGLN INVGCGATCV SNIKKAVKEQ KADLGISLDG
DADRIIIVDE NGQEIDGDGI LNILAQYSDI CGGTNGIVGT QMTNMSYENH YRANKIPFIR
SKVGDRYVLE DLVKYGYKIG GESSGHVINL NFGTTGDGLF TAIQLLAIFS QADKPVSEFK
LQGELMQQTL INVPLTKKVA REDLQKVASD VNDVEKRLGN RGRVLLRPSG TEPVLRVMVE
ADDKSLATNE AEYLVEKVKQ KLV
