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A4TEL0 (GLMM_MYCGI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:Mflv_4947
OrganismMycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens (strain ATCC 700033 / PYR-GCK)) [Complete proteome] [HAMAP]
Taxonomic identifier350054 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length445 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 – 445445Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000087770

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4TEL0 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: DF196783C60F7D98

FASTA44546,267
        10         20         30         40         50         60 
MARLFGTDGV RGVANRELTP ELAMALGSAA ARRLGRAGAT RRRVAVVGRD PRASGEMLEA 

        70         80         90        100        110        120 
AVIAGIAGEG VDTLRVGILP TPAVAYLTSA YDADFGVMIS ASHNPMPDNG IKIFGPGGHK 

       130        140        150        160        170        180 
LDDATEDRIE ELVHQGPGER PTGAGIGRVV DAEDALERYL RHVGKAATTR LDPLTVVVDC 

       190        200        210        220        230        240 
AHGAASVAAP RAYRAAGANV IPIHADPDGL NINDGCGSTH MESLRSAVVS YGADLGLAHD 

       250        260        270        280        290        300 
GDADRCLAVD AHGRVIDGDA IMVVLALAMQ QSGELVSDTL VATVMSNMGL HLAMRSADIE 

       310        320        330        340        350        360 
VRTTGVGDRY VLEELRAGQF SLGGEQSGHI VLPSFGTTGD GIVTGLRLMA RMAQTGRSLA 

       370        380        390        400        410        420 
DLAQPMQTLP QVLINVEVAD KTTVADAPSV RDAVAQVEAE LGDTGRILLR PSGTEQVVRV 

       430        440 
MVEAADEDTA RQMAVRVADS VSAES 

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PYR-GCK.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000656 Genomic DNA. Translation: ABP47413.1.
RefSeqYP_001136201.1. NC_009338.1.

3D structure databases

ProteinModelPortalA4TEL0.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4TEL0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000023718; EBMYCP00000023380; EBMYCG00000023713.
GeneID4976258.
GenomeReviewsGene locus Mflv_4947 in contig CP000656_GR.
KEGGmgi:Mflv_4947.
PATRIC18038152. VBIMycGil17082_5042.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
GeneTreeEBGT00050000015909.
HOGENOMHBG644964.
OMAGVGSTHL.
PhylomeDBA4TEL0.
ProtClustDBPRK14318.

Enzyme and pathway databases

BioCycMGIL350054:MFLV_4947-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_MYCGI
AccessionPrimary (citable) accession number: A4TEL0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 37 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