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Reviewed, UniProtKB/Swiss-Prot A8EQZ2 (GLMM_ARCB4)

Last modified February 9, 2010. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoglucosamine mutase
    EC=5.4.2.10
Gene names
Name: glmM
Ordered Locus Names: Abu_0081
OrganismArcobacter butzleri (strain RM4018) [Complete proteome] [HAMAP]
Taxonomic identifier367737 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeArcobacter

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 MF_01554

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554

Post-translational modification

Activated by phosphorylation By similarity. HAMAP 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-KW

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 MF_01554
PRO_1000068887

Sites

Active site991Phosphoserine intermediate By similarity
Metal binding991Magnesium; via phosphate group By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity

Amino acid modifications

Modified residue991Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8EQZ2-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 7B85095EF5E4B8CB

FASTA44448,636
        10         20         30         40         50         60 
MKLFGTDGVR GKAGDFLDAI TVLKLAKAAG IYFRKHSTTN KILVGKDTRR SGYMIENALV 

        70         80         90        100        110        120 
SGLTAVGYDV IQIGPMPTPA IAYLTESMRC DAGIMISASH NPFEDNGIKF FDNHGNKLNT 

       130        140        150        160        170        180 
TCEEEIENIF NDMDLMQSEQ VTGRDIGSSK RIDDVIGRYI VAIKSSFPKN LTLKGLRIIL 

       190        200        210        220        230        240 
DCANGAAYKV GPTILEELGA DVITINNKPN GFNINENCGA MHPETVSNLV KEYRADIGLA 

       250        260        270        280        290        300 
LDGDADRLVV IDEKGEIVDG DNLLGALSVY LKNENLLKGD ACVATVMSNK ALEDYLQKNK 

       310        320        330        340        350        360 
ISLFRSNVGD KYVLEVMKEK GINFGGEQSG HIIFSDIAKT GDGLASALQV LALIIKSGKK 

       370        380        390        400        410        420 
ASEILNPFSL YPQILHNMKV TEKIPLEQIT GLEEVLKPIR QKGLRDLIRY SGTENKIRLL 

       430        440 
LEGKNKKDVE DAMQTLIAFF KKAL 

« Hide

References

[1]"The complete genome sequence and analysis of the Epsilonproteobacterium Arcobacter butzleri."
Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.
PLoS ONE 2:E1358-E1358(2007) [PubMed: 18159241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000361 Genomic DNA. Translation: ABV66366.1.
RefSeqYP_001489035.1.

3D structure databases

SMRA8EQZ2. Positions 2-444.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8EQZ2.

Genome annotation databases

GeneID5624423.
GenomeReviewsGene locus Abu_0081 in contig CP000361_GR.
KEGGabu:Abu_0081.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAIVINDEP.

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. A-D-PHexomutase_N.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_ARCB4
AccessionPrimary (citable) accession number: A8EQZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: February 9, 2010
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents