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A0PXZ6 (GLMM_CLONN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 46. 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:NT01CX_1165
OrganismClostridium novyi (strain NT) [Complete proteome] [HAMAP]
Taxonomic identifier386415 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

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_0000301301

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PXZ6 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 351278F462C42564

FASTA44948,486
        10         20         30         40         50         60 
MGRLFGTDGV RGVANTELTA DLAFKLGRAG AFVLTEGTHK PKILVGMDTR ISGDMLEAAL 

        70         80         90        100        110        120 
VAGILSVGAE AICVGVVPTP AIAYLTRKYK ADAGVVISAS HNPVEYNGIK FFNKNGYKLK 

       130        140        150        160        170        180 
DELEDRIQSI IENNFEGVPS PTGENLGRKI TCESAIDDYV EFAKSTIDVD LKGLKIALDC 

       190        200        210        220        230        240 
ANGASYKTSV ETFRELGAEV VVINNDPDGV NINKNCGSTH PEELMDYVVK QGCDLGLAFD 

       250        260        270        280        290        300 
GDADRCLAVD EKGNLIDGDF IMTICGKHLK DQGKLKDNMV VVTVMSNLGL SLAFDKENIS 

       310        320        330        340        350        360 
TIKTKVGDRY VLEEMVKDGY KLGGEQSGHI IFLDYNTTGD GLVTGLQIAS IVKETGKTLS 

       370        380        390        400        410        420 
ELASIMTKLP QVLVNAKVPN NMKDIHEKDA EIAEEIKKIE EKLNGCGRVL IRPSGTEPLV 

       430        440 
RVMLEGENQE ELDKIAHALA KMIEEKANA

« Hide

References

[1]"The genome and transcriptomes of the anti-tumor agent Clostridium novyi-NT."
Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B., Zhou S.
Nat. Biotechnol. 24:1573-1580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000382 Genomic DNA. Translation: ABK61023.1.
RefSeqYP_877248.1. NC_008593.1.

3D structure databases

ProteinModelPortalA0PXZ6.
ModBaseSearch...

Protein-protein interaction databases

STRING386415.NT01CX_1165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK61023; ABK61023; NT01CX_1165.
GeneID4541926.
KEGGcno:NT01CX_1165.
PATRIC19477994. VBICloNov112828_0276.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMAEFAKSTI.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycCNOV386415:GH98-386-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. 3 hits.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_CLONN
AccessionPrimary (citable) accession number: A0PXZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 9, 2007
Last modified: May 1, 2013
This is version 46 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

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