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B0C132 (GLMM_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. 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:AM1_3435
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesAcaryochloris

Protein attributes

Sequence length455 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 – 455455Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000343583

Sites

Active site1061Phosphoserine intermediate By similarity
Metal binding1061Magnesium; via phosphate group By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity

Amino acid modifications

Modified residue1061Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0C132 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: F37595567FAD8AD8

FASTA45549,461
        10         20         30         40         50         60 
MAAAKDVNLF GTDGIRGHVG QHLTPQLALQ VGFCAGLELG QDASPHQPFI LGQDSRNSSD 

        70         80         90        100        110        120 
MLAMALSAGL TAAGLDVWHI GLCPTPTVAY LTHHTEAVGG VMVSASHNPP ADNGIKFFQA 

       130        140        150        160        170        180 
NGTKLPPTTQ GKIEQRIRAY SQQQPSGTWG HHFHRPELTK SYTDAIQTPL HAQVDFQGLK 

       190        200        210        220        230        240 
VVLDLAWGAA TQLAPAVFKA MGAEVICLHD QPDGDRINVN CGSTHLAPLK AAVNLHEADV 

       250        260        270        280        290        300 
GFAFDGDADR VLAIDCQGRT VDGDYILYLW GKALQQQNQL PKDLIVATVM SNLGFELAWQ 

       310        320        330        340        350        360 
QQGGTLLRAA VGDQNVHAEM LNHGSMLGGE QSGHILCPHY GVSGDGLLTA LHLATIICQN 

       370        380        390        400        410        420 
KTRLSCLVDD SFQTYPQLLK NVRVEDRDRR RNWQECQPLQ TLIDQATDDM GDQGRILVRA 

       430        440        450 
SGTEPLIRVM VEARDMRMVN HWTDQLVRAV ETHLA 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW28430.1.
RefSeqYP_001517746.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0C132.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0C132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5682244.
GenomeReviewsGene locus AM1_3435 in contig CP000828_GR.
KEGGamr:AM1_3435.
PATRIC20621110. VBIAcaMar40141_3183.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAGVGSTHL.
PhylomeDBB0C132.
ProtClustDBPRK14317.

Enzyme and pathway databases

BioCycAMAR329726:AM1_3435-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_ACAM1
AccessionPrimary (citable) accession number: B0C132
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 29 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