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A0JZ25 (GLMM_ARTS2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:Arth_2916
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length452 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_B

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554_B

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554_B

Post-translational modification

Activated by phosphorylation By similarity. HAMAP MF_01554_B

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: InterPro

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000301277

Sites

Active site1041Phosphoserine intermediate By similarity
Metal binding1041Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1041Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JZ25 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: D0D1E5E1EB62D4B1

FASTA45246,803
        10         20         30         40         50         60 
MSRLFGTDGV RGLANGLLTA ELAMQLAQAA AVVLGHERST NGARPRAVVA RDPRASGEFI 

        70         80         90        100        110        120 
SAAVSAGLSS SGIDVYDAGV LPTPAAAYLV ADLHADFGVM ISASHNPAPD NGIKFFAKGG 

       130        140        150        160        170        180 
QKLPDEVEDA IEAQMAKDPV RPTGSDVGRI QTFSDAEDRY IVHLLGTLPH RLDGLKVVLD 

       190        200        210        220        230        240 
CAHGAASGCS PQLFNDAGAE IVVIGAEPDG LNINDGVGST HLGALQRAVV EHGADLGIAH 

       250        260        270        280        290        300 
DGDADRCLAI DHEGNEVDGD QIMAILALAL KESGKLKDNV LVATVMSNLG LKIALRNAGI 

       310        320        330        340        350        360 
SIRETAVGDR YVLEEMRDGG YNLGGEQSGH VIFADHATTG DGLLTGLQLA AQVALTGKSL 

       370        380        390        400        410        420 
KELATVMTKL PQLMINVKKV DKARAGTDEG VLAAVAEASA ELGETGRVLL RPSGTEALVR 

       430        440        450 
VMVEAADMPT AERICKHLAA VVEERLAVAP AV 

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
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., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FB24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000454 Genomic DNA. Translation: ABK04295.1.
RefSeqYP_832395.1. NC_008541.1.

3D structure databases

ProteinModelPortalA0JZ25.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0JZ25.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4444403.
GenomeReviewsGene locus Arth_2916 in contig CP000454_GR.
KEGGart:Arth_2916.
PATRIC21001243. VBIArtSp72239_3304.
TIGRArth_2916.

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAGVGSTHL.
PhylomeDBA0JZ25.
ProtClustDBPRK14318.

Enzyme and pathway databases

BioCycASP1667:ARTH_2916-MONOMER.

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. Alpha-D-phosphohexomutase_SF.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KOK03431.
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. 2 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_ARTS2
AccessionPrimary (citable) accession number: A0JZ25
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 12, 2006
Last modified: January 25, 2012
This is version 40 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