Skip Header

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

A1SF29 (GLMM_NOCSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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

Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:Noca_0891
OrganismNocardioides sp. (strain BAA-499 / JS614) [Complete proteome] [HAMAP]
Taxonomic identifier196162 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaeNocardioidaceaeNocardioides

Protein attributes

Sequence length448 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 – 448448Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000301350

Sites

Active site1041Phosphoserine intermediate By similarity
Metal binding1041Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1041Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1SF29 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 3F4E858434969EAD

FASTA44846,469
        10         20         30         40         50         60 
MTRIFGTDGV RGLANGQLTA ELALDLSVAA ARVLADRGEF KGHRPLAVVG RDTRISGQFL 

        70         80         90        100        110        120 
EHAVVAGLAS AGVDVLRLRV LPTPAVAYLT EALGADLGVV ISASHNPMPD NGIKFLARGG 

       130        140        150        160        170        180 
HKLDDAVEKL IEQHLAEEWD RPVGGDVGRV TPYATPVEEY VAHLVGTLTR SLDGIKVVLD 

       190        200        210        220        230        240 
CAHGAAYEAG PRALRAAGAE VVAIAVEPDG LNINADCGST HLAALQAAVV EHGADVGFAL 

       250        260        270        280        290        300 
DGDADRCLAV DHEGNAVDGD QILAILALGM AETGHLAKNT VVATVMSNLG FVQAMRAAGV 

       310        320        330        340        350        360 
GVRQTKVGDR YVLEAMRVSG YSLGGEQSGH VIMSEHATTG DGILTALHVL QRMAATGQSL 

       370        380        390        400        410        420 
QSLASVVTRL PQVLVNVPDV DKSRADDDAV LAAAIAEEEA ALGDSGRVLL RPSGTEQLVR 

       430        440 
VMVEAATQEE AVSVAGRLAD VVKRQLAL 

« Hide

References

[1]"Complete sequence of chromosome 1 of Nocardioides sp. JS614."
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., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BAA-499 / JS614.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000509 Genomic DNA. Translation: ABL80414.1.
RefSeqYP_922101.1. NC_008699.1.

3D structure databases

ProteinModelPortalA1SF29.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1SF29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4599898.
GenomeReviewsGene locus Noca_0891 in contig CP000509_GR.
KEGGnca:Noca_0891.
PATRIC22743779. VBINocSp122728_1149.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAGVGSTHL.
PhylomeDBA1SF29.

Enzyme and pathway databases

BioCycNSP35761:NOCA_0891-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_NOCSJ
AccessionPrimary (citable) accession number: A1SF29
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 36 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