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Q15VJ3 (GLMM_PSEA6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. 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:Patl_1573
OrganismPseudoalteromonas atlantica (strain T6c / ATCC BAA-1087) [Complete proteome] [HAMAP]
Taxonomic identifier342610 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length447 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 – 447447Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000301357

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q15VJ3 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: C01C2C2BC8813E24

FASTA44747,479
        10         20         30         40         50         60 
MSDRKYFGTD GIRGKVGENL INPEFVMKLG WAAGKVLAGS GTNKVIIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALESGLSAAG INIGLLGPMP TPAIAYLTKT FRSEAGIVIS ASHNPYYDNG IKFFSADGSK 

       130        140        150        160        170        180 
LDDDIELAIE AEMDKPMQCV ASDKLGKAVR IADAAGRYIE FCKGNFPSNL SLKGLKIVVD 

       190        200        210        220        230        240 
CAHGATYHIA PNVLSELGAE VIEIGTEPDG LNINRKVGAT SMKAIVDSVI KHKADLGFAL 

       250        260        270        280        290        300 
DGDGDRIMLV DHHGNVIDGD QIVYIIARDA LKSGKLKGGV VGTVMSNLGL EVALSTLGVP 

       310        320        330        340        350        360 
FERSKVGDRY VLELLRQKGW SIGGEGSGHV LNLDAASTGD GIVAGLQVLA AMLNANMTLN 

       370        380        390        400        410        420 
ELSRGMTKFP QTLINVRFNE GDTPLDAQDV KNSVLEAESA LGERGRVLLR KSGTEPLIRV 

       430        440 
MVEANDATDS RKWAEHIADA VRKATGQ 

« Hide

References

[1]"Complete sequence of Pseudoalteromonas atlantica T6c."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T6c / ATCC BAA-1087.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000388 Genomic DNA. Translation: ABG40095.1.
RefSeqYP_661149.1. NC_008228.1.

3D structure databases

ProteinModelPortalQ15VJ3.
ModBaseSearch...

Protein-protein interaction databases

STRING342610.Patl_1573.

Proteomic databases

PRIDEQ15VJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG40095; ABG40095; Patl_1573.
GeneID4172565.
KEGGpat:Patl_1573.
PATRIC23048174. VBIPseAtl25434_1678.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycPATL342610:GHGT-1657-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_PSEA6
AccessionPrimary (citable) accession number: Q15VJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 25, 2006
Last modified: May 1, 2013
This is version 52 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