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Reviewed, UniProtKB/Swiss-Prot A1URA6 (GLMM_BARBK)

Last modified November 3, 2009. Version 25. 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: BARBAKC583_0171
OrganismBartonella bacilliformis (strain ATCC 35685 / KC583) [Complete proteome] [HAMAP]
Taxonomic identifier360095 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity.

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP 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: 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 – 450450Phosphoglucosamine mutase HAMAP MF_01554
PRO_0000301280

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity
Metal binding2481Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1URA6-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 22A2CBCC7764DA31

FASTA45049,421
        10         20         30         40         50         60 
MARKYFGTDG IRGKANIFPM TPDFAMKVGI AVGVLFRSKA TSRRVVIGKD TRLSCYMLEN 

        70         80         90        100        110        120 
ALVAGFTAAG MDAFLLGPIP TPAVAMLCRS LRADIGVMIS ASHNAFYDNG IKLFGPDGFK 

       130        140        150        160        170        180 
LSDEKETKIE ALLDSDISEL PLANCEEIGR AKRVEGDIYR YIEYAKRTLP RDVRLDALRI 

       190        200        210        220        230        240 
VVDCANGATY KAAPRALWEL GAEVIAINDE PNGFNINQEC GSTDLTSLRN KVHEVRADVG 

       250        260        270        280        290        300 
IALDGDGDRV LMVDEKGQMI DGDQLIAVIA EHWHKTGRLH HKGIVTTVMS NLGLERFLSE 

       310        320        330        340        350        360 
KGLKLIRTDV GDRYVVDMMR QKKYNIGGES SGHIILSDFC TTGDGLVAAL QVLACMKESQ 

       370        380        390        400        410        420 
QPMSQLCKRF EPVPQILKNK VVHNKNVLQK SEVQAALTKA SEHLGKEGRL LVRASGTEPV 

       430        440        450 
IRVMAEGDDR KAMTAIVDDL ITLIARHDHD 

« Hide

References

[1]Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., Fraser-Ligget C., Seshadri R.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000524 Genomic DNA. Translation: ABM45449.1.
RefSeqYP_988509.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1URA6.

Genome annotation databases

GeneID4683927.
GenomeReviewsGene locus BARBAKC583_0171 in contig CP000524_GR.
KEGGbbk:BARBAKC583_0171.
NMPDRfig|360095.3.peg.1127.
TIGRBARBAKC583_0171.

Phylogenomic databases

OMAVHDRYIE.

Family and domain databases

HAMAPMF_01554.
[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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_BARBK
AccessionPrimary (citable) accession number: A1URA6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 25 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