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Q8Q037 (GLMM_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 60. 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:
Probable phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:MM_0301
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length434 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. HAMAP-Rule MF_01554

Post-translational modification

Activated by phosphorylation By similarity. HAMAP-Rule MF_01554

Sequence similarities

Belongs to the phosphohexose mutase family.

Sequence caution

The sequence AAM29997.1 differs from that shown. Reason: Erroneous initiation.

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 – 434434Probable phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000337820

Sites

Active site911Phosphoserine intermediate By similarity
Metal binding911Magnesium; via phosphate group By similarity
Metal binding2291Magnesium By similarity
Metal binding2311Magnesium By similarity
Metal binding2331Magnesium By similarity

Amino acid modifications

Modified residue911Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Q037 [UniParc].

Last modified June 10, 2008. Version 2.
Checksum: 6B6C6857AAEFB508

FASTA43447,007
        10         20         30         40         50         60 
MKLFGSSGIR GIVNTEVTPE LALKVGLVLG SRKKTAVIGR DPRVSAPMIE HALVAGLTAA 

        70         80         90        100        110        120 
GCDVTKAGMV TTPTLAYAAR KYECGVMVTA SHNPSEYVGI KLWNPDGMAF DSAQQEEIEE 

       130        140        150        160        170        180 
AIEKENFSRV TWDLIGKIAE DENAIRDHMD MIEGLVGKSK LRVVLDCGCG AGSTITPYLL 

       190        200        210        220        230        240 
QELGCEIITL NSQPDGHFPA RNPEPNDQNL SLLKKAVVAF GADLGIAHDG DADRMMAVDE 

       250        260        270        280        290        300 
KGNFVSGDEL LAIFGRFECG DKKGSVVVPV DTSLMVDDYL EGSEIIRTRV GDVYVAEGIK 

       310        320        330        340        350        360 
QCKAIYGGEP SGSWIFPKIS YCPDGIYAAA KLVEIVNEKK LSELRAELPI YATKRGALPC 

       370        380        390        400        410        420 
ANEKKAEFMK RAKSKLEPLG KVLDIDGIRV ELENGWVLVR PSGTEAKVRI TAEARENVDG 

       430 
IYEMAEKIVK EALK 

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM29997.1. Different initiation.
RefSeqNP_632325.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ8Q037.
ModBaseSearch...

Protein-protein interaction databases

STRING192952.MM_0301.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM29997; AAM29997; MM_0301.
GeneID1478643.
KEGGmma:MM_0301.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268680.
KOK03431.
OMANANGMAY.
ProtClustDBCLSK811941.

Enzyme and pathway databases

BioCycMMAZ192952:GCK2-315-MONOMER.

Family and domain databases

Gene3D3.40.120.10. 3 hits.
HAMAPMF_01554_A. GlmM_A.
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.
IPR023666. GlmM_arc.
IPR024086. GlmM_arc-related.
[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. 3 hits.
TIGRFAMsTIGR03990. Arch_GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_METMA
AccessionPrimary (citable) accession number: Q8Q037
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: May 29, 2013
This is version 60 of the entry and version 2 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