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A5N4Y9 (GLMM_CLOK5) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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:CKL_0316
OrganismClostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680) [Complete proteome] [HAMAP]
Taxonomic identifier431943 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

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 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 – 449449Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000087762

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5N4Y9 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 5AF61F0D3D2EBAF5

FASTA44949,185
        10         20         30         40         50         60 
MHRMFGTDGV RGIANKELTP ELAYKLGKAG AYVLTGRCHK PKILVGMDTR ISGDMLENAL 

        70         80         90        100        110        120 
VSGILSIGAE AICVGIVPTP AVAYLTRKYN ADAGVVISAS HNPVEYNGIK FFNGKGYKLS 

       130        140        150        160        170        180 
DELEDKIQYV IESNFKDVSI PIGSKVGRKI METGEARKAY IEFAKSTIDT DLKDLKVVLD 

       190        200        210        220        230        240 
CANGASYVTS VKAFQELGAK VKVINNEPDG ININHNCGST HPENLMKTVV EEGYDMGLAF 

       250        260        270        280        290        300 
DGDADRCLAI DEKGNLINGD FIMAIIAKHL KNQGKLYKNV VVSTVMSNVG FDIALKEEGI 

       310        320        330        340        350        360 
NTIKTQVGDR YVLEEMRKEG YKLGGEQSGH IIMLDYNTTG DGLITALQIA CIVKKSGRKL 

       370        380        390        400        410        420 
SDIASMMKNL PQTLVNAKVP DDKKKIYMED EEIVLKIKEI ERKLHGCGRV LIRPSGTEPL 

       430        440 
VRVMLEGEEQ GEIDKMAHNL AELIEVKLN 

« Hide

References

[1]"The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features."
Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H., Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., Hagemeier C., Thauer R.K., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008) [PubMed: 18218779] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8527 / DSM 555 / NCIMB 10680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000673 Genomic DNA. Translation: EDK32370.1.
RefSeqYP_001393718.1. NC_009706.1.

3D structure databases

ProteinModelPortalA5N4Y9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5N4Y9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5391376.
GenomeReviewsGene locus CKL_0316 in contig CP000673_GR.
KEGGckl:CKL_0316.
NMPDRfig|431943.4.peg.347.
PATRIC19462025. VBICloKlu111549_0359.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMALGLDIAC.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycCKLU431943:CKL_0316-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_CLOK5
AccessionPrimary (citable) accession number: A5N4Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 36 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