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A1T554 (GLMM_MYCVP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 48. 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:Mvan_1472
OrganismMycobacterium vanbaalenii (strain DSM 7251 / PYR-1) [Complete proteome] [HAMAP]
Taxonomic identifier350058 [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-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 – 445445Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000301345

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
A1T554 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 602B8011060C556F

FASTA44546,106
        10         20         30         40         50         60 
MARLFGTDGV RGVANRELTA ELAMALGAAA ARRLGRTGAA RRRVAVVGRD PRASGEMLEA 

        70         80         90        100        110        120 
AVIAGIASEG VDTLRVGVLP TPAVAYLTSA YDADFGVMIS ASHNPMPDNG IKIFGPGGHK 

       130        140        150        160        170        180 
LDDATEDRIE ELVHQGPGSR PTGAGIGRVV DAEDALERYL RHVGKAATTR LDALTVVVDC 

       190        200        210        220        230        240 
AHGAASLAAP RAYRAAGANV IPIHAEPDGL NINDNCGSTH MQALSAAVVS YGADLGLAHD 

       250        260        270        280        290        300 
GDADRCLAVD AHGRVIDGDA IMVVLALAMQ EAGELASDTL VTTVMSNMGL HLAMRSAGIE 

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

       370        380        390        400        410        420 
GLAEPMQTLP QVLINVEVAD KATVADAQPV RDAVAQVEAE LGDTGRILLR PSGTEQVVRV 

       430        440 
MVEAADEDTA RQMAVRVAES VSAQR 

« Hide

References

[1]"Complete sequence of Mycobacterium vanbaalenii PYR-1."
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., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.J., Miller C., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 7251 / PYR-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000511 Genomic DNA. Translation: ABM12304.1.
RefSeqYP_952310.1. NC_008726.1.

3D structure databases

ProteinModelPortalA1T554.
ModBaseSearch...

Protein-protein interaction databases

STRING350058.Mvan_1472.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM12304; ABM12304; Mvan_1472.
GeneID4643329.
KEGGmva:Mvan_1472.
PATRIC18181161. VBIMycVan31953_1510.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK14318.

Enzyme and pathway databases

BioCycMVAN350058:GIWR-1481-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_MYCVP
AccessionPrimary (citable) accession number: A1T554
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 48 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