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A7FZ14 (GLMM_CLOB1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 41. 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:CLB_3477
OrganismClostridium botulinum (strain ATCC 19397 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier441770 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length449 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-Rule MF_01554

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP-Rule 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: HAMAP

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_1000068900

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7FZ14 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 43FE412B7F249257

FASTA44948,893
        10         20         30         40         50         60 
MGRMFGTDGV RGIANKELTA DLAYKLGKAG AFILTEGTHR SKILVGMDTR ISGDMLESAL 

        70         80         90        100        110        120 
VAGILSVGAE AICVGVIPTP AIAYLTRKYN ADAGVVISAS HNPVEYNGIK FFNKNGYKLS 

       130        140        150        160        170        180 
DELEDSIQAL IRDDFKDVPV LTGENIGRKI EEDGEAIRDY IDFAKSTIKG DLKGLKVALD 

       190        200        210        220        230        240 
CANGASYITS VEAFKELGAE VHVINNKPDG ININRNSGST HPEDLMEYVV KNNCHMGLAF 

       250        260        270        280        290        300 
DGDADRCLAI DEKGNLINGD FILAICGKEL KKQGRLKKNT IVVTVMSNLG LDIAMKKEEI 

       310        320        330        340        350        360 
NTIKTKVGDR YVLEEMLKND YAIGGEQSGH IIFSDYNTTG DGLVTALQLA HIVKESGKTF 

       370        380        390        400        410        420 
SELCSIMKEL PQVLVNAKVP NDQKDIYLKD EEIKSEIDTI TKNLDGSGRV LIRPSGTEPL 

       430        440 
VRVMLEGENQ KEIDKLAHGL AKLIENKVK

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References

[1]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19397 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000726 Genomic DNA. Translation: ABS35577.1.
RefSeqYP_001385737.1. NC_009697.1.

3D structure databases

ProteinModelPortalA7FZ14.
ModBaseSearch...

Protein-protein interaction databases

STRING441770.CLB_3477.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS35577; ABS35577; CLB_3477.
GeneID5394742.
KEGGcba:CLB_3477.
PATRIC19361496. VBICloBot110701_3352.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycCBOT441770:GH1E-3474-MONOMER.

Family and domain databases

Gene3D3.40.120.10. 3 hits.
HAMAPMF_01554_B. GlmM_B.
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]
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_CLOB1
AccessionPrimary (citable) accession number: A7FZ14
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 11, 2007
Last modified: May 1, 2013
This is version 41 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

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