GLMM_BACAN
ID GLMM_BACAN Reviewed; 448 AA.
AC Q81VN7; Q6I4N7; Q6KYD5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=BA_0157, GBAA_0157, BAS0158;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE016879; AAP24209.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29239.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT52494.1; -; Genomic_DNA.
DR RefSeq; NP_842723.1; NC_003997.3.
DR RefSeq; WP_000521474.1; NZ_WXXJ01000014.1.
DR RefSeq; YP_026443.1; NC_005945.1.
DR PDB; 3PDK; X-ray; 2.70 A; A/B=1-448.
DR PDBsum; 3PDK; -.
DR AlphaFoldDB; Q81VN7; -.
DR SMR; Q81VN7; -.
DR MINT; Q81VN7; -.
DR STRING; 261594.GBAA_0157; -.
DR DNASU; 1084111; -.
DR EnsemblBacteria; AAP24209; AAP24209; BA_0157.
DR EnsemblBacteria; AAT29239; AAT29239; GBAA_0157.
DR GeneID; 64201167; -.
DR KEGG; ban:BA_0157; -.
DR KEGG; bar:GBAA_0157; -.
DR KEGG; bat:BAS0158; -.
DR PATRIC; fig|198094.11.peg.154; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_0_9; -.
DR OMA; PHNPEPL; -.
DR BRENDA; 5.4.2.10; 634.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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 3D-structure; Isomerase; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..448
FT /note="Phosphoglucosamine mutase"
FT /id="PRO_0000147839"
FT ACT_SITE 100
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 100
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 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3PDK"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 20..35
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:3PDK"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:3PDK"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:3PDK"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:3PDK"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:3PDK"
FT HELIX 427..445
FT /evidence="ECO:0007829|PDB:3PDK"
SQ SEQUENCE 448 AA; 48417 MW; BC5DDEFCDB6D1920 CRC64;
MGKYFGTDGV RGVANKELTP ELAFKIGRFG GYVLTKDTDR PKVIIGRDTR ISGHMLEGAL
VAGLLSTGAE VMRLGVISTP GVAYLTKALD AQAGVMISAS HNPVQDNGIK FFGSDGFKLT
DEQEAEIEAL LDKEVDELPR PTGTNLGQVS DYFEGGQKYL QYIKQTVEED FSGLHIALDC
AHGATSSLAP YLFADLEADI STMGTSPNGM NINDGVGSTH PEVLAELVKE KGADIGLAFD
GDGDRLIAVD EKGNIVDGDQ IMFICAKYMK ETGQLKHNTV VSTVMSNLGF YKALEANGIT
SDKTAVGDRY VMEEMKRGGY NLGGEQSGHI ILLDYITTGD GMLSALQLVN IMKMTKKPLS
ELAGEMTKFP QLLVNVRVTD KKLALENEKI KEIIRVVEEE MNGDGRILVR PSGTEPLIRV
MAEAPTQEVC DAYVHRIVEV VKAEVGAE
