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Protein

Phosphoglucosamine mutase

Gene

glmM

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable).UniRule annotation1 Publication

Catalytic activityi

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei100 – 1001Phosphoserine intermediate
Metal bindingi100 – 1001Magnesium; via phosphate groupUniRule annotation
Metal bindingi240 – 2401MagnesiumUniRule annotation
Metal bindingi242 – 2421MagnesiumUniRule annotation
Metal bindingi244 – 2441MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU01770-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucosamine mutaseUniRule annotation (EC:5.4.2.10UniRule annotation)
Gene namesi
Name:glmMUniRule annotation
Synonyms:ybbT
Ordered Locus Names:BSU01770
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Phosphoglucosamine mutasePRO_0000147846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001PhosphoserineUniRule annotation

Post-translational modificationi

Activated by phosphorylation.UniRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO34824.

Expressioni

Inductioni

Constitutively expressed, part of the cdaA-cdaR-glmM-glmS operon (PubMed:23192352).1 Publication

Interactioni

Subunit structurei

Homodimer, may form a complex with CdaA.1 Publication

Protein-protein interaction databases

IntActiO34824. 1 interaction.
MINTiMINT-8367047.
STRINGi224308.Bsubs1_010100001008.

Structurei

3D structure databases

ProteinModelPortaliO34824.
SMRiO34824. Positions 3-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QJF. Bacteria.
COG1109. LUCA.
HOGENOMiHOG000268678.
InParanoidiO34824.
KOiK03431.
OMAiFNLGGEQ.
OrthoDBiEOG6TN467.
PhylomeDBiO34824.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
HAMAPiMF_01554_B. GlmM_B.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
IPR006352. GlmM_bact.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
TIGRFAMsiTIGR01455. glmM. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34824-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKYFGTDGV RGVANSELTP ELAFKVGRFG GYVLTKDKQR PKVLIGRDTR
60 70 80 90 100
ISGHMLEGAL VAGLLSIGAE VMRLGVISTP GVSYLTKAMD AEAGVMISAS
110 120 130 140 150
HNPVQDNGIK FFGGDGFKLS DEQEAEIERL MDEPEDKLPR PVGADLGLVN
160 170 180 190 200
DYFEGGQKYL QFLKQTADED FTGIHVALDC ANGATSSLAT HLFADLDADV
210 220 230 240 250
STMGTSPNGL NINDGVGSTH PEALSAFVKE KNADLGLAFD GDGDRLIAVD
260 270 280 290 300
EKGNIVDGDQ IMYICSKHLK SEGRLKDDTV VSTVMSNLGF YKALEKEGIK
310 320 330 340 350
SVQTAVGDRY VVEAMKKDGY NVGGEQSGHL IFLDYNTTGD GLLSAIMLMN
360 370 380 390 400
TLKATGKPLS ELAAEMQKFP QLLVNVRVTD KYKVEENEKV KAVISEVEKE
410 420 430 440
MNGDGRILVR PSGTEPLVRV MAEAKTKELC DEYVNRIVEV VRSEMGLE
Length:448
Mass (Da):48,433
Last modified:January 1, 1998 - v1
Checksum:iD13861BF333EFFA3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71T → K in BAA33070 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006424 Genomic DNA. Translation: BAA33070.1.
AL009126 Genomic DNA. Translation: CAB11953.1.
PIRiB69745.
RefSeqiNP_388058.1. NC_000964.3.
WP_003234946.1. NZ_JNCM01000030.1.

Genome annotation databases

EnsemblBacteriaiCAB11953; CAB11953; BSU01770.
GeneIDi938632.
KEGGibsu:BSU01770.
PATRICi18971907. VBIBacSub10457_0182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006424 Genomic DNA. Translation: BAA33070.1.
AL009126 Genomic DNA. Translation: CAB11953.1.
PIRiB69745.
RefSeqiNP_388058.1. NC_000964.3.
WP_003234946.1. NZ_JNCM01000030.1.

3D structure databases

ProteinModelPortaliO34824.
SMRiO34824. Positions 3-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO34824. 1 interaction.
MINTiMINT-8367047.
STRINGi224308.Bsubs1_010100001008.

Proteomic databases

PaxDbiO34824.

Protocols and materials databases

DNASUi938632.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11953; CAB11953; BSU01770.
GeneIDi938632.
KEGGibsu:BSU01770.
PATRICi18971907. VBIBacSub10457_0182.

Phylogenomic databases

eggNOGiENOG4107QJF. Bacteria.
COG1109. LUCA.
HOGENOMiHOG000268678.
InParanoidiO34824.
KOiK03431.
OMAiFNLGGEQ.
OrthoDBiEOG6TN467.
PhylomeDBiO34824.

Enzyme and pathway databases

BioCyciBSUB:BSU01770-MONOMER.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
HAMAPiMF_01554_B. GlmM_B.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
IPR006352. GlmM_bact.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
TIGRFAMsiTIGR01455. glmM. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the 70kb region between 17 and 23 degree of the Bacillus subtilis chromosome."
    Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
    Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
    Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: 168.
  4. "Cyclic di-AMP homeostasis in Bacillus subtilis: both lack and high level accumulation of the nucleotide are detrimental for cell growth."
    Mehne F.M., Gunka K., Eilers H., Herzberg C., Kaever V., Stuelke J.
    J. Biol. Chem. 288:2004-2017(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "An essential poison: synthesis and degradation of cyclic di-AMP in Bacillus subtilis."
    Gundlach J., Mehne F.M., Herzberg C., Kampf J., Valerius O., Kaever V., Stuelke J.
    J. Bacteriol. 197:3265-3274(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH CDAS.
    Strain: 168.

Entry informationi

Entry nameiGLMM_BACSU
AccessioniPrimary (citable) accession number: O34824
Secondary accession number(s): O87090
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 1, 1998
Last modified: April 13, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.