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Reviewed, UniProtKB/Swiss-Prot B6END8 (GLMM_ALISL)

Last modified November 3, 2009. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoglucosamine mutase
    EC=5.4.2.10
Gene names
Name: glmM
Ordered Locus Names: VSAL_I0594
OrganismAliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) [Complete proteome] [HAMAP]
Taxonomic identifier316275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity.

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Post-translational modification

Activated by phosphorylation By similarity.

Sequence similarities

Belongs to the phosphohexose mutase family.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Phosphoglucosamine mutase HAMAP MF_01554
PRO_1000201055

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B6END8-1 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: DEBD157B09568C77

FASTA44547,787
        10         20         30         40         50         60 
MAERKYFGTD GVRGLVGQSP ITPEFVMKLG WAAGKVLAKQ GTKKVIIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALEAGLAAAG LKAKFTGPMP TPAVAYLTQT FRAEAGIVIS ASHNPYYDNG IKFFSSEGTK 

       130        140        150        160        170        180 
LPDDVEMAIE AELDKPMTCV ESALLGKASR LNDAAGRYIE FCKSTFPKEL SLAGVKMVVD 

       190        200        210        220        230        240 
CAHGATYHIA PNVFKELGAE IITIGCEPNG TNINHEVGAT DVRALQAKVL EEKADFGVAF 

       250        260        270        280        290        300 
DGDGDRIIMV DDLGNKVDGD QIAYIIARDA LRRGELKGGV VGTLMTNMGM EVALRNLGIP 

       310        320        330        340        350        360 
FVRSNVGDRY VMEKLLENNW KIGAENSGHV ILLDKVTTGD AIVAALQVIA SIVGSKMSLK 

       370        380        390        400        410        420 
ELCNGMTLFP QVLENIRFVG DNNPLDTELV KAAQADVETK LGDNGRVLLR KSGTEPLIRV 

       430        440 
MVEGENAELV QQYALQIVDA VKESC 

« Hide

References

[1]"The complete genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238."
Hjerde E., Lorentzen M.S., Holden M.T.G., Seeger K., Paulsen S., Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., Thurston S., Parkhill J., Willassen N.-P., Thomson N.R.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

FM178379 Genomic DNA. Translation: CAQ78279.1.
RefSeqYP_002262114.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6988558.
GenomeReviewsGene locus VSAL_I0594 in contig FM178379_GR.
KEGGvsa:VSAL_I0594.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAVHDRYIE.

Family and domain databases

HAMAPMF_01554.
[Tree]
InterProIPR005844. 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. A-D-PHexomutase_N.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PfamPF02878. 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]
PRINTSPR00509. PGMPMM.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_ALISL
AccessionPrimary (citable) accession number: B6END8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: November 3, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents