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Q8YVS4 (GLMM_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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:alr1900
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length490 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.

Sequence caution

The sequence BAB73599.1 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: 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 – 490490Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000147836

Sites

Active site1391Phosphoserine intermediate By similarity
Metal binding1391Magnesium; via phosphate group By similarity
Metal binding2791Magnesium By similarity
Metal binding2811Magnesium By similarity
Metal binding2831Magnesium By similarity

Amino acid modifications

Modified residue1391Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YVS4 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 5C3C4D375092B360

FASTA49052,509
        10         20         30         40         50         60 
MVSSITRIQN YVIDGAATSN GLETVLESNF APSLISLPAT PLFGTDGIRG KVGELLSAPL 

        70         80         90        100        110        120 
ALQIGFWAGV VLRNHADQLG PVILGQDSRN SSDMLAMALS AGLTAAGLEV WYLGLCPTPC 

       130        140        150        160        170        180 
VAYLTSMSEA IGGVMISASH NPPEDNGIKI FGANGGKLSQ ALQAEIEKGL RGNLPITSNV 

       190        200        210        220        230        240 
SNCGRHYSRW ELVKNYGEAL KRPWQNKVNL QGMKVVLDLA WGAAVGLAPS VFAEMGAEVI 

       250        260        270        280        290        300 
SLHNAADGDR INVNCGSTHL EMLQAAVQEH NADLGFAFDG DADRVLAVDP TGRPVNGDYI 

       310        320        330        340        350        360 
LYLWGLYLKQ QNQLPDNLIV STVMANLGFE KAWQQQGGKL IRTAVGDQYV QAEMIKTGAM 

       370        380        390        400        410        420 
LGGEQSGHIL CSHYGMTGDG LLTALHLASL VKQSGVSLAE LIDQSFQTYP QLLRNVRVVD 

       430        440        450        460        470        480 
RDRRLSWQNC TPVQQAIALA EKAMGDTGRI LVRASGTEPV IRVMVEAANA ELANYWTNEL 

       490 
VAQVQQHLAP 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7120 / UTEX 2576.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000019 Genomic DNA. Translation: BAB73599.1. Different initiation.
PIRAF2043.
RefSeqNP_485940.1. NC_003272.1.

3D structure databases

ProteinModelPortalQ8YVS4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8YVS4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1105492.
GenomeReviewsGene locus alr1900 in contig BA000019_GR.
KEGGana:alr1900.
NMPDRfig|103690.1.peg.2207.
PATRIC22773888. VBINosSp37423_2420.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAGVGSTHL.
PhylomeDBQ8YVS4.
ProtClustDBPRK14317.

Enzyme and pathway databases

BioCycNSP103690:ALR1900-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_NOSS1
AccessionPrimary (citable) accession number: Q8YVS4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 25, 2012
This is version 54 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