GLMM_BACSU
ID GLMM_BACSU Reviewed; 448 AA.
AC O34824; O87090;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
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}; Synonyms=ybbT;
GN OrderedLocusNames=BSU01770;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT Bacillus subtilis chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [4]
RP INDUCTION.
RX PubMed=23192352; DOI=10.1074/jbc.m112.395491;
RA Mehne F.M., Gunka K., Eilers H., Herzberg C., Kaever V., Stuelke J.;
RT "Cyclic di-AMP homeostasis in Bacillus subtilis: both lack and high level
RT accumulation of the nucleotide are detrimental for cell growth.";
RL J. Biol. Chem. 288:2004-2017(2013).
RN [5]
RP SUBUNIT, AND INTERACTION WITH CDAS.
RC STRAIN=168;
RX PubMed=26240071; DOI=10.1128/jb.00564-15;
RA Gundlach J., Mehne F.M., Herzberg C., Kampf J., Valerius O., Kaever V.,
RA Stuelke J.;
RT "An essential poison: synthesis and degradation of cyclic di-AMP in
RT Bacillus subtilis.";
RL J. Bacteriol. 197:3265-3274(2015).
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is
CC used for cell wall biosynthesis (Probable). {ECO:0000255|HAMAP-
CC Rule:MF_01554, ECO:0000305|PubMed:26240071}.
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 -!- SUBUNIT: Homodimer, may form a complex with CdaA.
CC {ECO:0000269|PubMed:26240071}.
CC -!- INDUCTION: Constitutively expressed, part of the cdaA-cdaR-glmM-glmS
CC operon (PubMed:23192352). {ECO:0000269|PubMed:23192352}.
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; AB006424; BAA33070.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11953.1; -; Genomic_DNA.
DR PIR; B69745; B69745.
DR RefSeq; NP_388058.1; NC_000964.3.
DR RefSeq; WP_003234946.1; NZ_JNCM01000030.1.
DR PDB; 7OJR; X-ray; 3.05 A; A=1-448.
DR PDB; 7OJS; X-ray; 4.20 A; A/B/C/F/G/J=1-369.
DR PDB; 7OLH; X-ray; 3.65 A; A/B/C/D/E/F=1-448.
DR PDB; 7OML; X-ray; 2.90 A; A=1-448.
DR PDBsum; 7OJR; -.
DR PDBsum; 7OJS; -.
DR PDBsum; 7OLH; -.
DR PDBsum; 7OML; -.
DR AlphaFoldDB; O34824; -.
DR SASBDB; O34824; -.
DR SMR; O34824; -.
DR IntAct; O34824; 1.
DR MINT; O34824; -.
DR STRING; 224308.BSU01770; -.
DR jPOST; O34824; -.
DR PaxDb; O34824; -.
DR PRIDE; O34824; -.
DR DNASU; 938632; -.
DR EnsemblBacteria; CAB11953; CAB11953; BSU_01770.
DR GeneID; 938632; -.
DR KEGG; bsu:BSU01770; -.
DR PATRIC; fig|224308.179.peg.183; -.
DR eggNOG; COG1109; Bacteria.
DR InParanoid; O34824; -.
DR OMA; PHNPEPL; -.
DR PhylomeDB; O34824; -.
DR BioCyc; BSUB:BSU01770-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IBA:GO_Central.
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:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
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_0000147846"
FT ACT_SITE 100
FT /note="Phosphoserine intermediate"
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 CONFLICT 7
FT /note="T -> K (in Ref. 1; BAA33070)"
FT /evidence="ECO:0000305"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:7OML"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:7OML"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:7OJR"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:7OML"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 371..377
FT /evidence="ECO:0007829|PDB:7OML"
FT TURN 381..384
FT /evidence="ECO:0007829|PDB:7OJR"
FT HELIX 390..401
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:7OML"
FT STRAND 413..423
FT /evidence="ECO:0007829|PDB:7OML"
FT HELIX 427..444
FT /evidence="ECO:0007829|PDB:7OML"
SQ SEQUENCE 448 AA; 48433 MW; D13861BF333EFFA3 CRC64;
MGKYFGTDGV RGVANSELTP ELAFKVGRFG GYVLTKDKQR PKVLIGRDTR ISGHMLEGAL
VAGLLSIGAE VMRLGVISTP GVSYLTKAMD AEAGVMISAS HNPVQDNGIK FFGGDGFKLS
DEQEAEIERL MDEPEDKLPR PVGADLGLVN DYFEGGQKYL QFLKQTADED FTGIHVALDC
ANGATSSLAT HLFADLDADV STMGTSPNGL NINDGVGSTH PEALSAFVKE KNADLGLAFD
GDGDRLIAVD EKGNIVDGDQ IMYICSKHLK SEGRLKDDTV VSTVMSNLGF YKALEKEGIK
SVQTAVGDRY VVEAMKKDGY NVGGEQSGHL IFLDYNTTGD GLLSAIMLMN TLKATGKPLS
ELAAEMQKFP QLLVNVRVTD KYKVEENEKV KAVISEVEKE MNGDGRILVR PSGTEPLVRV
MAEAKTKELC DEYVNRIVEV VRSEMGLE
