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Reviewed, UniProtKB/Swiss-Prot Q1IV19 (GLMM_ACIBL)

Last modified November 3, 2009. Version 25. 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: Acid345_0276
OrganismAcidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]
Taxonomic identifier204669 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaCandidatus Koribacter

Protein attributes

Sequence length463 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 – 463463Phosphoglucosamine mutase HAMAP MF_01554
PRO_0000305629

Sites

Active site1101Phosphoserine intermediate By similarity
Metal binding1101Magnesium; via phosphate group By similarity
Metal binding2551Magnesium By similarity
Metal binding2571Magnesium By similarity
Metal binding2591Magnesium By similarity

Amino acid modifications

Modified residue1101Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IV19-1 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: FA6947AA9FD18FA0

FASTA46349,676
        10         20         30         40         50         60 
MSLPTMDKPV RQLFGTDGIR GVAGEYPLDP HTVFAIGRAL GARLVEKYQT ARVLIGQDTR 

        70         80         90        100        110        120 
ESSDWISRAL ARGLESANCG VASAGVITTP GVAYLTRTHG FSAGIVVSAS HNPWTDNGIK 

       130        140        150        160        170        180 
VFGANGYKLS DDIEHEIEAQ IFYHLEELER AESEGEGPAM LPGDDKLRED YAEWLRSQVE 

       190        200        210        220        230        240 
GTDFSKFRVL LDCANGAASS IAHLVFPKVG VFSEFTHICP TGRNINANCG ALHPEEAAKH 

       250        260        270        280        290        300 
VGQSRGRFDL GITFDGDADR ALFSDGDGNI VNGDAVLLLA ARDMKARGHL KEDTVVATTM 

       310        320        330        340        350        360 
SNMGLEAALK RSGIRMLRAA VGDKYVLEEM KKTGATLGGE QSGHILFMDS DATTGDGILT 

       370        380        390        400        410        420 
ALRVLEVLAR SGKSLAELIA DLKVFPQVIR NVKVNAKIPM KELPAVMSAI EAAEQDLGDS 

       430        440        450        460 
GRVVVRYSGT EKLARVMIEA ESEAKMNQHA TAIAEAIQEA IGI 

« Hide

Cross-references

Sequence databases

CP000360 Genomic DNA. Translation: ABF39281.1.
RefSeqYP_589355.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ1IV19.

Genome annotation databases

GeneID4068820.
GenomeReviewsGene locus Acid345_0276 in contig CP000360_GR.
KEGGaba:Acid345_0276.
NMPDRfig|204669.6.peg.268.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1IV19.
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_ACIBL
AccessionPrimary (citable) accession number: Q1IV19
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 13, 2006
Last modified: November 3, 2009
This is version 25 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