Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot B7ICC7 (GLMM_ACIB5)

Last modified October 13, 2009. Version 9. 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: AB57_3769
OrganismAcinetobacter baumannii (strain AB0057) [Complete proteome] [HAMAP]
Taxonomic identifier480119 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

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_1000201048

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
B7ICC7-1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: B74CEC00715EF4B2

FASTA44548,162
        10         20         30         40         50         60 
MSYFGTDGIR GKFGQMPITP EFALKLGFAA GKVLKRTSPK NKPLVVLGKD TRLSGYILES 

        70         80         90        100        110        120 
ALQAGLNAAG VYVHLLGPLP TPAIAHLTRA LHAHAGIVIS ASHNPYFDNG IKFFSSEGKK 

       130        140        150        160        170        180 
LPDSLQEEIN KELEKDLFIE DTANLGKSVR VTDANGRYIE FCKSTFPYHF DLNNLKIVVD 

       190        200        210        220        230        240 
CAHGAAYSVG PSVFRELGAK VVALYNEPDG LNINENCGST HPESLQKAVV EHGADLGIAF 

       250        260        270        280        290        300 
DGDADRVVMV DKFGNLIDGD HILYILATQA KNKPAGVVGT VMSNMALEVA LEKANVGFVR 

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

       370        380        390        400        410        420 
NGFKLYPQVL VNVRLEQMLD PYSIPALVAE FNKAEEQLKG RGRILIRKSG TEPVIRVMVE 

       430        440 
GDNEQEVKTL AEHLANAVRS QAQVA 

« Hide

References

[1]"Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii."
Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., Bonomo R.A., Gill S.R.
J. Bacteriol. 190:8053-8064(2008) [PubMed: 18931120] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001182 Genomic DNA. Translation: ACJ43121.1.
RefSeqYP_002321057.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7043750.
GenomeReviewsGene locus AB57_3769 in contig CP001182_GR.
KEGGabn:AB57_3769.

Organism-specific databases

CMRSearch...

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_ACIB5
AccessionPrimary (citable) accession number: B7ICC7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: October 13, 2009
This is version 9 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