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Reviewed, UniProtKB/Swiss-Prot A8HUR7 (GLMM_AZOC5)

Last modified November 3, 2009. Version 15. 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: AZC_0975
OrganismAzorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / ORS 571) [Complete proteome] [HAMAP]
Taxonomic identifier438753 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeAzorhizobium

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_1000073569

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8HUR7-1 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 7750C3E539B19C1A

FASTA44748,485
        10         20         30         40         50         60 
MARKYFGTDG VRGRANATLT ADLALRVGMA AGLAFRRGEH RHRVVIGKDT RLSGYMIENA 

        70         80         90        100        110        120 
LVAGFTSVGM DVLLLGPMPT PAVGMLTRSM RADLGVMISA SHNPFDDNGI KLFGPDGFKL 

       130        140        150        160        170        180 
SDQIEHEIEE LIDEDLSKKL AQPMDIGRAR RVEGVHARYI EYAKRTLPRD QSFEGLRVVV 

       190        200        210        220        230        240 
DCANGAAYRV APDALWELGA EVISMGVEPD GLNINRDVGS TSPAALSAKV REVRADVGIA 

       250        260        270        280        290        300 
LDGDADRVII VDEKGHVVDG DQIMAVVAHS FKEDGRLSRD GIVATVMSNL GLERYLKDEG 

       310        320        330        340        350        360 
LTLARTSVGD RYVLERMRSD GYNVGGEQSG HIILSDYSTT GDGLLAALQV LAVVARSERP 

       370        380        390        400        410        420 
VSEVCHRFDP LPQVLKNVRY SSGKPLEHEN VQSAIADAER RLANHGRLLI RPSGTEPVIR 

       430        440 
VMGEGDDFEL VEGVVDEVIE ALRKVAA 

« Hide

References

[1]"Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium caulinodans ORS571."
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP009384 Genomic DNA. Translation: BAF86973.1.
RefSeqYP_001523891.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5690551.
GenomeReviewsGene locus AZC_0975 in contig AP009384_GR.
KEGGazc:AZC_0975.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMASTHPEAM.

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_AZOC5
AccessionPrimary (citable) accession number: A8HUR7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 4, 2007
Last modified: November 3, 2009
This is version 15 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