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A5FWQ4 (GLMM_ACICJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. 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:Acry_0817
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length456 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. HAMAP-Rule MF_01554

Post-translational modification

Activated by phosphorylation By similarity. HAMAP-Rule MF_01554

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: UniProtKB-HAMAP

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000318616

Sites

Active site1091Phosphoserine intermediate By similarity
Metal binding1091Magnesium; via phosphate group By similarity
Metal binding2501Magnesium By similarity
Metal binding2521Magnesium By similarity
Metal binding2541Magnesium By similarity

Amino acid modifications

Modified residue1091Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FWQ4 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 6D6298EA9A5A8EC6

FASTA45647,614
        10         20         30         40         50         60 
MNQIQPRPKR RLFGTDGIRG RANTAPMTAE IALRLGQAAG LLFTRGDHRH RVIIGKDTRL 

        70         80         90        100        110        120 
SGYMLEPALT AGFIGAGMDV TLAGPLPTPA IAMLTRSLRA DLGVVISASH NPFEDNGIKL 

       130        140        150        160        170        180 
FGPDGAKLSD ETEAEIEALM EEDLSGRLAA PSALGRAMRL VDAAGRYVES AKSSLPRGLR 

       190        200        210        220        230        240 
LDGLRVVLDC ANGAAYKVAP AALWELGAEV ITLGVSPDGF NINHECGSTV PSALSAAVVK 

       250        260        270        280        290        300 
HRADLGIALD GDADRVILAD ERGRIIDGDQ VLALIARAFQ ADGRLSGSGI VATVMSNLGL 

       310        320        330        340        350        360 
ERYLGGLGLA LHRTPVGDRY VAEHMRAHGL NLGGEQSGHV ILADFATTGD GLIAALQVLA 

       370        380        390        400        410        420 
VLVREGRPAS EVCRLFTPLP QLLRNVRYSG ASPLLSPAVT AAAAAAEARL AGIGRLLLRA 

       430        440        450 
SGTEPLIRVM AEGEDEQLVA AVVDELCAVI EAESAG 

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
US DOE Joint Genome Institute
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., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000697 Genomic DNA. Translation: ABQ30036.1.
RefSeqYP_001233955.1. NC_009484.1.

3D structure databases

ProteinModelPortalA5FWQ4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349163.Acry_0817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ30036; ABQ30036; Acry_0817.
GeneID5161695.
KEGGacr:Acry_0817.
PATRIC20646616. VBIAciCry6074_1305.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMAHTTGDGI.
OrthoDBEOG6TN467.
ProtClustDBPRK14315.

Enzyme and pathway databases

BioCycACRY349163:GHET-829-MONOMER.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 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. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_ACICJ
AccessionPrimary (citable) accession number: A5FWQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 49 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