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C3K264 (GLMM_PSEFS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 30. 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:PFLU_5258
OrganismPseudomonas fluorescens (strain SBW25) [Complete proteome] [HAMAP]
Taxonomic identifier216595 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

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_1000215495

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
C3K264 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 46522149472A702E

FASTA44547,750
        10         20         30         40         50         60 
MTKKYFGTDG IRGRVGEFPI TPDFMLKLGW AAGMAFRSMG ACRILVGKDT RISGYMFESA 

        70         80         90        100        110        120 
LEAGLSAAGA DVMLLGPMPT PAIAYLTRTF HAEAGIVISA SHNPHDDNGI KFFSGQGTKL 

       130        140        150        160        170        180 
PDEIELMIEE LLDAPMTVVE SSKLGKVSRI NDASGRYIEF CKSSVPSSTN FAGLKIVVDC 

       190        200        210        220        230        240 
AHGATYKVAP SVFKELGADV TVLSAQPNGL NINDNCGSTH MEQLQAAVLA EHADLGIAFD 

       250        260        270        280        290        300 
GDGDRVLMVD HTGAIVDGDD LLFIIARDLH ERNKLQGGVV GTLMSNLGLE LALADLGIPF 

       310        320        330        340        350        360 
VRANVGDRYV IAELLERNWQ VGGENSGHVV CFQHTTTGDA IIAALQVLLS LRRREESLAQ 

       370        380        390        400        410        420 
ARQALRKCPQ VLLNVRFAGG ENPIEHPAVK EACERVTLAM AGRGRVLLRK SGTEPLVRVM 

       430        440 
VEGDDETQVR GHAEDLAKLV TEVCA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM181176 Genomic DNA. Translation: CAY52358.1.
RefSeqYP_002874760.1. NC_012660.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING216595.PFLU5258.

Proteomic databases

PRIDEC3K264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAY52358; CAY52358; PFLU_5258.
GeneID7821131.
KEGGpfs:PFLU5258.
PATRIC19904636. VBIPseFlu98510_5390.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK10887.

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_PSEFS
AccessionPrimary (citable) accession number: C3K264
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: May 1, 2013
This is version 30 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