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A8M4B8 (GLMM_SALAI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:Sare_4252
OrganismSalinispora arenicola (strain CNS-205) [Complete proteome] [HAMAP]
Taxonomic identifier391037 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora

Protein attributes

Sequence length451 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 – 451451Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000343595

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8M4B8 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: B8CA8636A0745EDD

FASTA45146,358
        10         20         30         40         50         60 
MGRLFGTDGV RGRANADLTP ELALAVAVAA AHTLAEADRS HPPLAVVGRD TRASGEMLEA 

        70         80         90        100        110        120 
AVVAGLTSAG ANVVRVGVLP TPAVAFLTAE AKADFGVMLS ASHNPMPDNG IKLFAAGGHK 

       130        140        150        160        170        180 
LPDEIEMKIE AAIEANATTA WERPVGAGVG RVHDLLDGAD HYVQHLVGTV PHRLDGIKVV 

       190        200        210        220        230        240 
VDCANGAAAE VAPAAYREAG AEVVEIHAKP DGLNINDECG SNHLAALQQA VVEHGAQLGI 

       250        260        270        280        290        300 
AHDGDADRCV AVSADGDEVD GDQVMAILAL AMRQAGTLTA DTLVATVMSN LGLRIAMSRE 

       310        320        330        340        350        360 
GIRLVETKVG DRYVLEELRA SGLALGGEQS GHIVMPAHAT TGDGVLTGLH LMSRLAATGK 

       370        380        390        400        410        420 
SLAELAAVVT PLPQVLINVP VGDRTVGAVA PAVRAEVERA EVELGDAGRV LLRPSGTEPL 

       430        440        450 
VRVMVEASTE TLARQVAERI ADQVRTASPV G 

« Hide

References

[1]"Complete sequence of Salinispora arenicola CNS-205."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K. expand/collapse author list , Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNS-205.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000850 Genomic DNA. Translation: ABW00034.1.
RefSeqYP_001539024.1. NC_009953.1.

3D structure databases

ProteinModelPortalA8M4B8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8M4B8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5704384.
GenomeReviewsGene locus Sare_4252 in contig CP000850_GR.
KEGGsaq:Sare_4252.
PATRIC23437087. VBISalAre38676_4292.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAGVGSTHL.
ProtClustDBPRK14318.

Enzyme and pathway databases

BioCycSARE391037:SARE_4252-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_SALAI
AccessionPrimary (citable) accession number: A8M4B8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: December 4, 2007
Last modified: January 25, 2012
This is version 31 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