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Q086H7 (GLMM1_SHEFN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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 1

EC=5.4.2.10
Gene names
Name:glmM1
Ordered Locus Names:Sfri_0985
OrganismShewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP]
Taxonomic identifier318167 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length445 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 – 445445Phosphoglucosamine mutase 1 HAMAP MF_01554_B
PRO_0000305672

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
Q086H7 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: AAD3ADEB8A8A2E98

FASTA44547,829
        10         20         30         40         50         60 
MKQRKFFGTD GIRGRVGAGK MTPELALKLG WAAGRVLSRN GTQKVIIGKD TRISGYLFES 

        70         80         90        100        110        120 
ALEAGLSAAG LNVLLLGPMP TPAVAYLTRT FRAEAGVVIS ASHNPYYDNG IKFFSTDGSK 

       130        140        150        160        170        180 
LDDAIELEIE AELEKPLVCV ESHLLGKARR IEDAAGRYIE YCKGNFPADQ TLEGLKIVVD 

       190        200        210        220        230        240 
CAHGATYHIA PNVFRELGAD VIAIGDKPDG LNINDKVGAT SMAKICETVL AEKADLGIAL 

       250        260        270        280        290        300 
DGDGDRIMMV NRHGEVVDGD QILYILAVDA QKRGILKGGV VGTLMSNLGL DLALQALDIP 

       310        320        330        340        350        360 
FVRSKVGDRY VMEMLRENEW RIGGENSGHI LNLDHGTTGD GIVAGILVLA AMRRQNASLE 

       370        380        390        400        410        420 
QLTEPMKMLP QVLVNVRFEG DSNPLDTDAV KSAQADVELQ LGARGRVLLR KSGTEPLIRV 

       430        440 
MVEGDDHPQV LAHANRIADA VKAAC 

« Hide

References

[1]"Complete sequence of Shewanella frigidimarina NCIMB 400."
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., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., Newman D., Tiedje J.M. expand/collapse author list , Zhou J., Romine M.F., Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCIMB 400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000447 Genomic DNA. Translation: ABI70838.1.
RefSeqYP_749676.1. NC_008345.1.

3D structure databases

ProteinModelPortalQ086H7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ086H7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4278202.
GenomeReviewsGene locus Sfri_0985 in contig CP000447_GR.
KEGGsfr:Sfri_0985.
NMPDRfig|318167.10.peg.938.
PATRIC23495821. VBISheFri14343_1019.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAIGSAKRI.
PhylomeDBQ086H7.
ProtClustDBPRK10887.

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 nameGLMM1_SHEFN
AccessionPrimary (citable) accession number: Q086H7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 31, 2006
Last modified: January 25, 2012
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