Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q2RGA6 (GLMM_MOOTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase
EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:Moth_2246
OrganismMoorella thermoacetica (strain ATCC 39073) [Reference proteome] [HAMAP]
Taxonomic identifier264732 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteraceae › Moorella group › Moorella ›

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-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
Reference 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 – 444444Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000301339

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RGA6 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 6E96893725712904

FASTA44446,170
        10         20         30         40         50         60 
MGKLFGTDGV RGVANQGLPP ELAFRLGRAG AAVLAGKGDR VRVVVGRDTR ISGDMLEAAL 

        70         80         90        100        110        120 
VAGICSVGGQ VLKVGIIPTP AVAWLTRDLG ADAGVVISAS HNPVADNGIK FFSASGYKLP 

       130        140        150        160        170        180 
DPVEEEIERL VLAPEDNLPR PVGVDLGRVK EVTEAPERYI AHVCSTAGRG LAGMQVVLDC 

       190        200        210        220        230        240 
ANGAACRVAP AIFQRLGAEV SLLHNVPDGT NINVRCGSTH PESLQAEVVA RGAAVGLAFD 

       250        260        270        280        290        300 
GDADRVIAVD EKGQVVDGDV IMTILALYRQ EQGGLPGGQV VVTVMSNYGL HQALTAAGLR 

       310        320        330        340        350        360 
VQQTRVGDRY VLEEMLKSGA VLGGEQSGHI ILLEHNTTGD GLITGVQLLQ VMAATGRPLS 

       370        380        390        400        410        420 
ELAAAMPRLP QILVNVRVGD KDAAMASPAL QAAVAAAREQ LAGRGRVLVR PSGTEPIIRL 

       430        440 
MVEGPDREEL ENIMAGLQRV ASGL

« Hide

References

[1]"The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)."
Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.
Environ. Microbiol. 10:2550-2573(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39073.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000232 Genomic DNA. Translation: ABC20533.1.
RefSeqYP_431076.1. NC_007644.1.

3D structure databases

HSSPHSSP built from PDB template 2FKF based on UniProtKB P26276.
ProteinModelPortalQ2RGA6.
ModBaseSearch...

Protein-protein interaction databases

STRING264732.Moth_2246.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC20533; ABC20533; Moth_2246.
GeneID3830741.
KEGGmta:Moth_2246.
PATRIC22641954. VBIMooThe6753_2445.

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.

Enzyme and pathway databases

BioCycMTHE264732:GH0A-2337-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_MOOTA
AccessionPrimary (citable) accession number: Q2RGA6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 24, 2006
Last modified: May 1, 2013
This is version 54 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents