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Q6A6T5 (GLMM_PROAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. 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:PPA1801
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium ›

Protein attributes

Sequence length450 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 – 450450Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000147936

Sites

Active site1041Phosphoserine intermediate By similarity
Metal binding1041Magnesium; via phosphate group By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity

Amino acid modifications

Modified residue1041Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6A6T5 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 97EEBA9D00924783

FASTA45047,631
        10         20         30         40         50         60 
MARLFGTDGV RGVANQDLTA ELALDLSVAA AHVLGEAGAF GHRQPTALVA RDPRASGEFL 

        70         80         90        100        110        120 
EAAVCAGLAS AGVDVLRVGV IPTPAAAYLV NEYRTDLGVM LSASHNPMPD NGIKFFSRGG 

       130        140        150        160        170        180 
VKLPDDLEDA IEQRMGEPWA RPIGDKVGRI RYTPQAVDTY VDHLVRSLRQ QDTLKGMKIV 

       190        200        210        220        230        240 
LDTANGASFH TATAAFTTQG AEVIAIHDQP DGLNINERCG STHPEKLQAK VVEVGADMGL 

       250        260        270        280        290        300 
AFDGDADRCL AVDHEGNIVD GDHIIAILAL ALQEDHRLAS NTVVATIMSN LGLIIAMRAH 

       310        320        330        340        350        360 
DIHVDQTKVG DRYVLESMNA NGFSLGGEQS GHVIMSEFAT TGDGVLTGLH LAARVARTGK 

       370        380        390        400        410        420 
TLKELASVMT RLPQALINVR GVDKLRAGID PDVNKAVADA NQKLGDAGRV VLRPSGTEPV 

       430        440        450 
VRVMVEAGTQ EEADQICSEL AETVKMSLAL

« Hide

References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017283 Genomic DNA. Translation: AAT83528.1.
RefSeqYP_056486.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6A6T5.
ModBaseSearch...

Protein-protein interaction databases

STRING267747.PPA1801.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT83528; AAT83528; PPA1801.
GeneID2932001.
KEGGpac:PPA1801.
PATRIC23038421. VBIProAcn64440_1860.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBCLSK2764186.

Enzyme and pathway databases

BioCycPACN267747:GHO9-1833-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. 2 hits.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_PROAC
AccessionPrimary (citable) accession number: Q6A6T5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: September 13, 2004
Last modified: May 1, 2013
This is version 58 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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