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B1XXG0 (GLMM_LEPCP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:Lcho_2815
OrganismLeptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6)) [Complete proteome] [HAMAP]
Taxonomic identifier395495 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesLeptothrix

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_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 – 444444Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000201115

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1XXG0 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 46A371CB69EB2756

FASTA44447,655
        10         20         30         40         50         60 
MSRKYFGTDG IRGEVGTSPI TPDFVLRLGH AVGRVLRGTH DRPVVLIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALEAGLNSAG VDVMLTGPLP TPAVAYLTRA LRLSLGVVIS ASHNHFMDNG IKFFSARGEK 

       130        140        150        160        170        180 
LSDAWEMEVE AAIEAPPQWS DSSQIGRARR LHDAPGRYVE FCKSTFSNEL SLKGLKIVVD 

       190        200        210        220        230        240 
AANGAAYHVA PDVFHELGAD VVRIGCEPDG LNINDGVGAT SPQALVEAVR MNGADYGVAL 

       250        260        270        280        290        300 
DGDADRVLLV DRNGRLYNGD ELLYVMVADR LAQGEPVPGA VGTLMTNMAV EVALQQRGVE 

       310        320        330        340        350        360 
FVRAKVGDRY VLEELVSRGW QLGGEGSGHL LALDKHTTGD GIVSALQVLQ AQQRNGRSIA 

       370        380        390        400        410        420 
ELLDGVELFP QTLINVRLAA GQDWKLNDRL ARERIAIGNE LGQSGRVLIR PSGTEPLLRV 

       430        440 
MVEARDAAQA RLCADRLAVA AQEG 

« Hide

References

[1]"Complete sequence of Leptothrix cholodnii SP-6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Emerson D., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001013 Genomic DNA. Translation: ACB35080.1.
RefSeqYP_001791845.1. NC_010524.1.

3D structure databases

ProteinModelPortalB1XXG0.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1XXG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6161656.
GenomeReviewsGene locus Lcho_2815 in contig CP001013_GR.
KEGGlch:Lcho_2815.
PATRIC22396037. VBILepCho83238_2845.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAESTDNIM.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycLCHO395495:LCHO_2815-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.
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. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_LEPCP
AccessionPrimary (citable) accession number: B1XXG0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 28 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