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A8MJD2 (GLMM_ALKOO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 37. 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:Clos_2382
OrganismAlkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) [Complete proteome] [HAMAP]
Taxonomic identifier350688 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length449 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-Rule MF_01554

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP-Rule 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: HAMAP

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_1000068886

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8MJD2 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 432F9834F010E456

FASTA44948,663
        10         20         30         40         50         60 
MGKLFGTDGV RGIANRDLTP ELAYQLGRIG AYVLNKDNNK RAKVAIGKDT RISGDLLESA 

        70         80         90        100        110        120 
MTAGFLSMGV DVISLGVLPT PAVAYLTRHL KADFGVVISA SHNPAEYNGI KFFNREGYKL 

       130        140        150        160        170        180 
PDEVEEQIEA YILNNRDVDI RMEGKDVGTV TVDEKSIEEY TDFLKTTLDR DFKGLKIAVD 

       190        200        210        220        230        240 
AGNGAAYRSA PKLLKELGAE VILINDTPDG MNINKGCGST NPEVIGALVK EVGADIGISF 

       250        260        270        280        290        300 
DGDADRLIAV DENGEVVDGD HIMAICGICL KKQGKLKNDV IVGTVMSNIG LEIAMKEYGC 

       310        320        330        340        350        360 
NVVKTKVGDR YVLEEMVQGG YCLGGEQSGH VIFLDYNTTG DGLLTAIQLI ATMKAENKKL 

       370        380        390        400        410        420 
SELAKVMTSY PQVLVNAKVK NENKEVYQND AIIMQSITAI ENKLAGEGRV LIRPSGTEPL 

       430        440 
VRVMLEGKNQ EELNVLATDL AKLIEQRLN 

« Hide

References

[1]"Complete genome of Alkaliphilus oremlandii OhILAs."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OhILAs.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000853 Genomic DNA. Translation: ABW19914.1.
RefSeqYP_001513910.1. NC_009922.1.

3D structure databases

ProteinModelPortalA8MJD2.
ModBaseSearch...

Protein-protein interaction databases

STRING350688.Clos_2382.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW19914; ABW19914; Clos_2382.
GeneID5676907.
KEGGaoe:Clos_2382.
PATRIC20870138. VBIAlkOre124042_2495.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycAORE350688:GHBG-2495-MONOMER.

Family and domain databases

Gene3D3.40.120.10. 3 hits.
HAMAPMF_01554_B. GlmM_B.
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]
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_ALKOO
AccessionPrimary (citable) accession number: A8MJD2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 4, 2007
Last modified: May 1, 2013
This is version 37 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