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Reviewed, UniProtKB/Swiss-Prot A6VP84 (GLMM_ACTSZ)

Last modified November 3, 2009. Version 19. 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: Asuc_1422
OrganismActinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]
Taxonomic identifier339671 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length444 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 – 444444Phosphoglucosamine mutase HAMAP MF_01554
PRO_1000073568

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
A6VP84-1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 5D557141BF9406D8

FASTA44447,437
        10         20         30         40         50         60 
MAERKYFGTD GVRGKVGSFP ITPDFALKLG WAAGKVLATH GSKKVLIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALEAGLTAAG LSAVFVGPMP TPAVAYLTRT FRAEAGVVIS ASHNPYDDNG IKFFSAEGTK 

       130        140        150        160        170        180 
LPDDVEEAIE ALLEQPMDCV ESAELGKASR INDAAGRYIE FCKSTFPTSL SLEGYKIVVD 

       190        200        210        220        230        240 
CAHGATYHIA PSVLRELGAE IIEIGTKPNG LNINEKCGAT DIEALRHKVL EIGADVGLAY 

       250        260        270        280        290        300 
DGDGDRIMMV DHLGNKVDGD QILYIIARET LRAGHLKGGV VGTLMSNMSL EIALKQLGIP 

       310        320        330        340        350        360 
FLRANVGDRY VLEKMQENGW KLGGENSGHI IILDKNTTGD GIIASLAVLT AMAQHKLSLH 

       370        380        390        400        410        420 
ELTGAVKLFP QVLINVRFAG GENPLNSEKV KAVAAEVEQR LAGKGRILLR KSGTEPLIRV 

       430        440 
MVECEDAVLA QKSAEEIAEA VKNS 

« Hide

References

[1]"Complete sequence of Actinobacillus succinogenes 130Z."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000746 Genomic DNA. Translation: ABR74781.1.
RefSeqYP_001344716.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA6VP84.

Genome annotation databases

GeneID5349178.
GenomeReviewsGene locus Asuc_1422 in contig CP000746_GR.
KEGGasu:Asuc_1422.

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_ACTSZ
AccessionPrimary (citable) accession number: A6VP84
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: November 3, 2009
This is version 19 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