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Reviewed, UniProtKB/Swiss-Prot Q6F717 (GLMM_ACIAD)

Last modified February 9, 2010. Version 41. 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: ACIAD3502
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity. HAMAP MF_01554

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554

Post-translational modification

Activated by phosphorylation By similarity. HAMAP MF_01554

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 – 443443Phosphoglucosamine mutase HAMAP MF_01554
PRO_0000147834

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
Q6F717-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 164458B5CA6B3E66

FASTA44348,181
        10         20         30         40         50         60 
MSYFGTDGIR GKFGEMPITP EFALKLGFAA GKVLKRTSPI NKPIVVLGKD TRLSGYILES 

        70         80         90        100        110        120 
ALQAGLNAAG VYVHLLGPLP TPAIAHLTRA LHADAGIVIS ASHNPYFDNG IKFFSGEGKK 

       130        140        150        160        170        180 
LPDSLQDEIN QELEHELHIE DTANLGKSVR LIDANGRYIE FCKSTFPYHF DLRNLTIVVD 

       190        200        210        220        230        240 
CANGAAYNVG PSVFRELGAK VIALYNDPNG MNINEHCGST HPENLQKAVV HYKADLGIAF 

       250        260        270        280        290        300 
DGDADRVILV DKFGELVDGD HILYILATQA KKKPAGIVGT VMSNMALELA LAKADVPFIR 

       310        320        330        340        350        360 
AKVGDRYVLQ ALEENDWVTG GEPSGHILTL DKSTTGDAII AALQVLTVMV EQNKALHELV 

       370        380        390        400        410        420 
TGFELFPQVL VNVRLDQMMD PYSVPALVSE FEQAEAQLKG RGRLLIRKSG TEPVIRVMVE 

       430        440 
GDNQKEVTDL AHRLAESVRT HAA 

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR543861 Genomic DNA. Translation: CAG70148.1.
RefSeqYP_047970.1.

3D structure databases

SMRQ6F717. Positions 2-441.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6F717.

Genome annotation databases

GeneID2881137.
GenomeReviewsGene locus ACIAD3502 in contig CR543861_GR.
KEGGaci:ACIAD3502.
NMPDRfig|62977.3.peg.3163.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMASTHPEAM.
PhylomeDBQ6F717.

Enzyme and pathway databases

BioCycASP62977:ACIAD3502-MONOMER.

Family and domain databases

HAMAPMF_01554_B. GlmM_B.
[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_ACIAD
AccessionPrimary (citable) accession number: Q6F717
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 19, 2004
Last modified: February 9, 2010
This is version 41 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