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Reviewed, UniProtKB/Swiss-Prot A0KNE8 (GLMM_AERHH)

Last modified November 3, 2009. Version 24. 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: AHA_3310
OrganismAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]
Taxonomic identifier380703 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length444 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 – 444444Phosphoglucosamine mutase HAMAP MF_01554
PRO_0000305632

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0KNE8-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 0F69EA63E0ECEEE1

FASTA44447,638
        10         20         30         40         50         60 
MARKYFGTDG VRGKVGEYPI TPDFVMKLGW AAGKVLSKKG TRKVLIGKDT RISGYMLESA 

        70         80         90        100        110        120 
LEAGLSAAGL KAILMGPMPT PAVAYLTRTF RAEAGIVISA SHNPYYDNGI KFFSADGTKL 

       130        140        150        160        170        180 
PDEVEMAIEA ELDHELKCVE SAELGKALRI DDAAGRYIEF CKSTFPSNLS LEGLKMVVDC 

       190        200        210        220        230        240 
GHGATYHIAP SVFRELGAEV IAIGCSPDGL NINDGVGSTA PEALAAKVLE CKADLGVAFD 

       250        260        270        280        290        300 
GDGDRLVMVD NTGYIIDGDE ILYIIARDAL RNGRLKGGVV GTLMANMGLE LALQTLGIPF 

       310        320        330        340        350        360 
ARAKVGDRYV LEMMNEKGWR IGGENSGHII CLDQTTTGDG IVAALQVLTA ICTAEMPLAK 

       370        380        390        400        410        420 
LRSGMNKFPQ VLVNVRFAEG RDPLAADAVQ QEVAKVEQEL AGRGRVLLRK SGTEPLIRVM 

       430        440 
VEGEHEQQVR DMAQRIAQQV ESAF 

« Hide

References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000462 Genomic DNA. Translation: ABK38205.1.
RefSeqYP_857799.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0KNE8.

Genome annotation databases

GeneID4490972.
GenomeReviewsGene locus AHA_3310 in contig CP000462_GR.
KEGGaha:AHA_3310.
TIGRAHA_3310.

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. 1 hit.
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_AERHH
AccessionPrimary (citable) accession number: A0KNE8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 12, 2006
Last modified: November 3, 2009
This is version 24 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