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Reviewed, UniProtKB/Swiss-Prot B4RXA8 (GLMM_ALTMD)

Last modified November 3, 2009. Version 12. 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: MADE_01688
OrganismAlteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]
Taxonomic identifier314275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

Protein attributes

Sequence length447 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 – 447447Phosphoglucosamine mutase HAMAP MF_01554
PRO_1000201056

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
B4RXA8-1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 55AF17CCDAEEEF98

FASTA44747,842
        10         20         30         40         50         60 
MTQRKYFGTD GIRGKVGESN INPEFVTKLG WAAGKVLAGR GTNKVLIGKD TRISGYMLES 

        70         80         90        100        110        120 
SLEAGLSAAG INIGLLGPMP TPAIAYLTKT FRSEAGIVIS ASHNPFYDNG IKFFSAQGFK 

       130        140        150        160        170        180 
LDDDIELAIE AMLEQPMTCV ASDKLGKATR INDAAGRYIE FCKGTFPSEL SLTGLKIVVD 

       190        200        210        220        230        240 
CAHGATYHIA PNVLRELGAT VIELGTTPDG LNINDGVGAT SMKAIVEKVK ESGADLGFAL 

       250        260        270        280        290        300 
DGDGDRIMMV DHLGNVLDGD QIVYIIARDA LKNGKMQGGV VGTLMSNLGL ENALSKLGVP 

       310        320        330        340        350        360 
FARSNVGDRY VMELLQQKGW SIGGENSGHV LNLNMSSTGD GIVAGLQVLA AMLRSHMDLH 

       370        380        390        400        410        420 
DLASGFDMYP QTLVNVRYTN QDIDYLAHAD VQNAKQEAEL ALGKTGRVLL RKSGTEPLIR 

       430        440 
VMVESNDEAQ SHKWAEHIAE TVRNLAN 

« Hide

References

[1]"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
ISME J. 2:1194-1212(2008) [PubMed: 18670397] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001103 Genomic DNA. Translation: ACG65992.1.
RefSeqYP_002125986.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6775619.
GenomeReviewsGene locus MADE_01688 in contig CP001103_GR.
KEGGamc:MADE_01688.

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_ALTMD
AccessionPrimary (citable) accession number: B4RXA8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: November 3, 2009
This is version 12 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