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Reviewed, UniProtKB/Swiss-Prot A1K5A1 (GLMM_AZOSB)

Last modified November 3, 2009. Version 22. 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: azo1389
OrganismAzoarcus sp. (strain BH72) [Complete proteome] [HAMAP]
Taxonomic identifier62928 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzoarcus

Protein attributes

Sequence length451 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 – 451451Phosphoglucosamine mutase HAMAP MF_01554
PRO_0000301278

Sites

Active site1071Phosphoserine intermediate By similarity
Metal binding1071Magnesium; via phosphate group By similarity
Metal binding2461Magnesium By similarity
Metal binding2481Magnesium By similarity
Metal binding2501Magnesium By similarity

Amino acid modifications

Modified residue1071Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1K5A1-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 0C6B090762F57776

FASTA45148,059
        10         20         30         40         50         60 
MARKYFGTDG VRGRVGELPI TPEFVMRLGY AAGVTLVARE HLPAGERPAI LIGKDTRVSG 

        70         80         90        100        110        120 
YMLEAALQAG FAAAGVDVLL AGPIPTPAVA YLTRALRLQA GVVISASHNP FYDNGIKFFS 

       130        140        150        160        170        180 
AGGAKLPDAV EAEIEERIGQ PMGCAESARL GRARRIGDAA GRYIEFCKSS FPNELDLRGL 

       190        200        210        220        230        240 
RIALDCAHGA AYHIAPNVFH ELGAEVISVG VDPNGLNIND GVGATRPENL RQAVLSHGAD 

       250        260        270        280        290        300 
LGIALDGDGD RLIMVDRQGE IYDGDKLLYV IASARAAEGR LDGVVGTLMS NLGFEHALER 

       310        320        330        340        350        360 
RGVAFARAKV GDRYVLEMLH ERGWKIGGEN SGHIICLDCH TTGDGIISAL QVLAALKHRE 

       370        380        390        400        410        420 
MSLSEACKDL VFYPQRLINV RLPAGFDWKA DARIAQTAAD AERTLGDTGR VLLRPSGTEP 

       430        440        450 
LLRVMVEGRD EQLVESLARG IAGAVELAVA G 

« Hide

References

[1]"Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72."
Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S. expand/collapse author list , Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.
Nat. Biotechnol. 24:1385-1391(2006) [PubMed: 17057704] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM406670 Genomic DNA. Translation: CAL94006.1.
RefSeqYP_932893.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1K5A1.

Genome annotation databases

GeneID4608823.
GenomeReviewsGene locus azo1389 in contig AM406670_GR.
KEGGazo:azo1389.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMASTHPEAM.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_AZOSB
AccessionPrimary (citable) accession number: A1K5A1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 22 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