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B8F5R2 (GLMM_HAEPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 33. 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:HAPS_1045
OrganismHaemophilus parasuis serovar 5 (strain SH0165) [Complete proteome] [HAMAP]
Taxonomic identifier557723 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus ›

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
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_1000185370

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8F5R2 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 136FBB8F1616C3E7

FASTA44447,132
        10         20         30         40         50         60 
MAERKYFGTD GVRGKVGQFP ITPDFALKLG WAAGKVLATQ GSKQVLIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALEAGLAAAG LSAAFTGPMP TPAIAYLTRT FRAEAGIVIS ASHNPYDDNG IKFFSAIGEK 

       130        140        150        160        170        180 
LPDEVEEAIE AMLDQPMDCV ESAELGRASR INDAAGRYIE FCKSTFPSHL SLDGYKIVVD 

       190        200        210        220        230        240 
CANGATYHIA PNVMRELGAE VIEIGTHPNG LNINEKCGAT DIKALQQVVV EAGADVGLAY 

       250        260        270        280        290        300 
DGDGDRLIMV DHLGNKVDGD QILFIIAREA LCSGKLHGGV VGTLMSNMSL ELALKELAIP 

       310        320        330        340        350        360 
FARANVGDRY VLEVLKEKGW KLGGENSGHI IVLDKNTTGD GIVASLEVLA AMASHKLSLN 

       370        380        390        400        410        420 
DLAKAVPLFP QVLINVRFAG GANPLDSEDV KAVAKAVEQR LAGKGRILLR KSGTEPLIRV 

       430        440 
MVECEDGALA QSCAEEISEA VKRN

« Hide

References

[1]"Complete genome sequence of Haemophilus parasuis SH0165."
Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R., Jin M., Jin Q., Chen H.
J. Bacteriol. 191:1359-1360(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH0165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001321 Genomic DNA. Translation: ACL32664.1.
RefSeqYP_002475612.1. NC_011852.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING557723.HAPS_1045.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL32664; ACL32664; HAPS_1045.
GeneID7277113.
KEGGhap:HAPS_1045.
PATRIC20194367. VBIHaePar127548_1040.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycHPAR557723:GH24-1045-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_HAEPS
AccessionPrimary (citable) accession number: B8F5R2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 1, 2013
This is version 33 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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