Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q0A772 (GLMM_ALHEH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:Mlg_1973
OrganismAlkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

Protein attributes

Sequence length451 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 – 451451Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000301273

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0A772 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 80FE8581598C2E82

FASTA45147,692
        10         20         30         40         50         60 
MKKEYFGTDG IRGTVGEPPI TPDFMLHLGW AAGRVLARAG QSSVLVGKDT RISGYMLESA 

        70         80         90        100        110        120 
LESGFAAAGV NVKLLGPMPT PAIAYLTRTL RAAAGVVISA SHNPHEDNGI KFFSDDGEKL 

       130        140        150        160        170        180 
DDATELAIEA ELRQPLKPAP SARLGKASRI NDAPGRYIEF CKRSFPYELS LRGLRLVVDC 

       190        200        210        220        230        240 
ANGATYHVAP AVFHELGAEV IPLADDPDGL NINADCGSLH PKGLQAAVRE HDADAGIAFD 

       250        260        270        280        290        300 
GDGDRVIMVD HRGEVVDGDG LLYIIARQRM ANGGLAGPVV GTVMSNLGLE QGIGRLGLPF 

       310        320        330        340        350        360 
LRAKVGDRYV MEMLRREGGI LGGESSGHLI CLDRTTTGDG IVSALQVLEA MAAQERTLAE 

       370        380        390        400        410        420 
LADGMDRLPQ IMVNVPISRG VPVQDHATVT DAVRDAETRL AGRGRVLLRP SGTEPVLRVM 

       430        440        450 
VEGPDQAEVS ATAEAIAGAV REAHATLTAP R 

« Hide

References

[1]"Complete sequence of Alkalilimnicola ehrilichei MLHE-1."
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., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MLHE-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000453 Genomic DNA. Translation: ABI57315.1.
RefSeqYP_742805.1. NC_008340.1.

3D structure databases

ProteinModelPortalQ0A772.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0A772.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4268516.
GenomeReviewsGene locus Mlg_1973 in contig CP000453_GR.
KEGGaeh:Mlg_1973.
NMPDRfig|187272.6.peg.1880.
PATRIC20863199. VBIAlkEhr114327_1968.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAGVGSTHL.
PhylomeDBQ0A772.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycAEHR187272:MLG_1973-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. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_ALHEH
AccessionPrimary (citable) accession number: Q0A772
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 17, 2006
Last modified: January 25, 2012
This is version 39 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