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A4FPG9 (GLMM_SACEN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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:SACE_6779
OrganismSaccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP]
Taxonomic identifier405948 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora

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_0000301375

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2391Magnesium By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4FPG9 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: E002C4C830DBDEA6

FASTA44446,036
        10         20         30         40         50         60 
MSRLFGTDGV RGLANADLTP ELALSVASAA ARVLYERDDS RRRVALVGRD PRASGEMLEA 

        70         80         90        100        110        120 
AVTAGLTSAG ADVLRVGVLP TPAVAHLVSA MRADLGVMIS ASHNPMPDNG IKLFAAGGHK 

       130        140        150        160        170        180 
LPDAVEDEIA DRLDERVDRP TGAAVGRARD VPDAGSRYVD HLLEATPQPL DGLRVVVDCA 

       190        200        210        220        230        240 
NGAAAAVAPS AYRLAGAEVI ALNAEPDGLN INEGVGSTHL DGLRAAVREH RADLGLAHDG 

       250        260        270        280        290        300 
DADRCLAVDA TGSVVDGDQI MAILAVAMKE AGELADDTLV TTVMSNLGLH LAMREHGVKL 

       310        320        330        340        350        360 
RTTAVGDRYV LAELREGGFS LGGEQSGHVV LPDHATTGDG LLTALRLMGR VVETGRSLAE 

       370        380        390        400        410        420 
LAATMTRLPQ VLVNVRVADK ATACGAPEVA KAVAEAEAEL GDEGRVLLRP SGTEQLVRVM 

       430        440 
VEARSEGTAQ RVAGRLAELV AAIR 

« Hide

References

[1]"Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
Nat. Biotechnol. 25:447-453(2007) [PubMed: 17369815] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NRRL 23338.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM420293 Genomic DNA. Translation: CAM05944.1.
RefSeqYP_001108869.1. NC_009142.1.

3D structure databases

ProteinModelPortalA4FPG9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4FPG9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4946509.
GenomeReviewsGene locus SACE_6779 in contig AM420293_GR.
KEGGsen:SACE_6779.
PATRIC23420998. VBISacEry28377_6781.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAGVGSTHL.
ProtClustDBCLSK2536777.

Enzyme and pathway databases

BioCycSERY405948:SACE_6779-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_SACEN
AccessionPrimary (citable) accession number: A4FPG9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: April 17, 2007
Last modified: December 14, 2011
This is version 36 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