(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 122.
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}.
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   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; BSU01770.
DR   GeneID; 938632; -.
DR   KEGG; bsu:BSU01770; -.
DR   PATRIC; fig|224308.179.peg.183; -.
DR   eggNOG; ENOG4107QJF; Bacteria.
DR   eggNOG; COG1109; LUCA.
DR   HOGENOM; HOG000268678; -.
DR   InParanoid; O34824; -.
DR   KO; K03431; -.
DR   OMA; MFGEEYT; -.
DR   PhylomeDB; O34824; -.
DR   BioCyc; BSUB:BSU01770-MONOMER; -.
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;
DR   PRODOM; O34824.
DR   SWISS-2DPAGE; O34824.
KW   Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..448
FT                   /note="Phosphoglucosamine mutase"
FT                   /id="PRO_0000147846"
FT   ACT_SITE        100
FT                   /note="Phosphoserine intermediate"
FT   METAL           100
FT                   /note="Magnesium; via phosphate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   METAL           240
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   METAL           242
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   METAL           244
FT                   /note="Magnesium"
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"
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
//

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