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A1AVH5 (GLMM_RUTMC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. 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:Rmag_0138
OrganismRuthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP]
Taxonomic identifier413404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length441 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 – 441441Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000305669

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2391Magnesium By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1AVH5 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: B962AF1CF3CE59B3

FASTA44147,935
        10         20         30         40         50         60 
MDNYFGTDGM RGKVGVEPIT ADFFLKLGWA VGSVLAKRAK ASVIIGKDTR VSGYLFESAL 

        70         80         90        100        110        120 
EAGFLSAGVD VGLLGPMPTP AVAYLTQTYN ASAGVVISAS HNNFQDNGVK FFSAKGLKLS 

       130        140        150        160        170        180 
SQYQSEIEKK LAETMISVGA DKIGKAYRYE QPLGRYIEFC KSTFDRTQSL LGLNIVIDCA 

       190        200        210        220        230        240 
NGATYHIAQS VFSELGANIN IINNTPDGFN INEHCGATDT KYLQQVVLES KADLGIAFDG 

       250        260        270        280        290        300 
DGDRLIMIDE NGELVDGDEL VFIIAKAWQS QGRLVNNTVV GTKMSNLGMH HALRDLDIKF 

       310        320        330        340        350        360 
IEADVGDRFV MEKMQKSGSI LGGEGSGHII CLNKTTSGDG IISALQVLEV LVKSQSSLAK 

       370        380        390        400        410        420 
LKQSMEKYPQ ILINVKTQAR INLKNYTKLQ RTQLAVEQTL GDESRVLIRV SGTEPLIRVM 

       430        440 
VEAKDKIIAQ QGAEKLSNIF K 

« Hide

References

[1]"The Calyptogena magnifica chemoautotrophic symbiont genome."
Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.
Science 315:998-1000(2007) [PubMed: 17303757] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000488 Genomic DNA. Translation: ABL01932.1.
RefSeqYP_903403.1. NC_008610.1.

3D structure databases

ProteinModelPortalA1AVH5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1AVH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4555386.
GenomeReviewsGene locus Rmag_0138 in contig CP000488_GR.
KEGGrma:Rmag_0138.
PATRIC31999861. VBICanRut45856_0162.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAESTDNIM.
PhylomeDBA1AVH5.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycCRUT413404:RMAG_0138-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.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_RUTMC
AccessionPrimary (citable) accession number: A1AVH5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: January 23, 2007
Last modified: December 14, 2011
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