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A3N2A2 (GLMM_ACTP2) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:APL_1454
OrganismActinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]
Taxonomic identifier416269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity. HAMAP MF_01554_B

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554_B

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554_B

Post-translational modification

Activated by phosphorylation By similarity. HAMAP MF_01554_B

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: InterPro

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000301271

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
A3N2A2 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: AA09923726E63D68

FASTA44447,313
        10         20         30         40         50         60 
MAERKYFGTD GVRGKVGQFP ITPDFALKLG WAAGKILATQ GTKQVLIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALEAGLAAAG LSAAFVGPMP TPAIAYLTRT FRAEAGIVIS ASHNPYYDNG IKFFSSVGEK 

       130        140        150        160        170        180 
LPDEVEEAIE ALLDQPMDCV ESAQLGKAMR INDAAGRYIE FCKGTFPANA SLKGYKIVVD 

       190        200        210        220        230        240 
CANGATYHIA PNVMRELGAE VIEIGTKPDG LNINEKCGAT DIKALQKVVV ESGADVGLAY 

       250        260        270        280        290        300 
DGDGDRIMMV DHLGNKVDGD QILFIIAREA LRSGKLHGGV VGTLMSNMGL EVALKHLAIP 

       310        320        330        340        350        360 
FTRANVGDRY VLEQLKEKGW KLGGENSGHI IVLDKNTTGD GIIASLEVLA AMEAHKMSLN 

       370        380        390        400        410        420 
DLARAVPLFP QVLINVRFEG GKNPLESDAV KAVAADVEKR LAGKGRILLR KSGTEPLIRV 

       430        440 
MVECEDGALA QSCAEEIVEA VKSN 

« Hide

References

[1]"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)."
Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E.
J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000569 Genomic DNA. Translation: ABN74538.1.
RefSeqYP_001054143.1. NC_009053.1.

3D structure databases

ProteinModelPortalA3N2A2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3N2A2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4849540.
GenomeReviewsGene locus APL_1454 in contig CP000569_GR.
KEGGapl:APL_1454.
PATRIC20747895. VBIActPle94089_1513.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAGVGSTHL.
PhylomeDBA3N2A2.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycAPLE416269:APL_1454-MONOMER.

Family and domain databases

HAMAPMF_01554_B. GlmM_B.
[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. Alpha-D-phosphohexomutase_SF.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KOK03431.
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.
SUPFAMSSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_ACTP2
AccessionPrimary (citable) accession number: A3N2A2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: April 3, 2007
Last modified: December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families