Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q12QI6 (GLMM_SHEDO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:Sden_1002
OrganismShewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) [Complete proteome] [HAMAP]
Taxonomic identifier318161 [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 HAMAP MF_01554_B
PRO_0000301376

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
Q12QI6 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 021CB37B86A925C9

FASTA44547,654
        10         20         30         40         50         60 
MKQRQFFGTD GIRGKVGAGK MTPELALKLG WAAGRVLSRT GTKKVIIGKD TRISGYLFES 

        70         80         90        100        110        120 
ALEAGLSAAG LNVLLVGPMP TPAVAYLTRT FRAEAGIVIS ASHNPYYDNG IKFFSTDGSK 

       130        140        150        160        170        180 
LDDAIELEIE AELEKPLTCV ESHLLGKAKR IDDAAGRYIE YCKGNFPADQ TLEGLKIVVD 

       190        200        210        220        230        240 
CAHGATYHIA PSVFSELGAE VIAIGDKPNG TNINHEVGAT SMGKICETVL AEGADLGIAL 

       250        260        270        280        290        300 
DGDGDRIMMV NRKGEVIDGD QILYILAADA QKRGQLKGGV VGTLMSNLGL DLALQALDIP 

       310        320        330        340        350        360 
FLRSNVGDRY VMEMLKKNDW RIGGENSGHI LDLDHGTTGD GIVAGILVLA AMRRQNATLE 

       370        380        390        400        410        420 
QLVEPMKMLP QVLINVRFEG SNNPLDSDLV KSAQREVEQS LGARGRVLLR KSGTEPLIRV 

       430        440 
MVEGDDHDLV LAHANRIAAA VKLGC 

« Hide

References

[1]"Complete sequence of Shewanella denitrificans OS217."
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., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS217 / ATCC BAA-1090 / DSM 15013.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000302 Genomic DNA. Translation: ABE54290.1.
RefSeqYP_562013.1. NC_007954.1.

3D structure databases

ProteinModelPortalQ12QI6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ12QI6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4017599.
GenomeReviewsGene locus Sden_1002 in contig CP000302_GR.
KEGGsdn:Sden_1002.
NMPDRfig|318161.14.peg.984.
PATRIC23487724. VBISheDen79529_1062.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAIGSAKRI.
PhylomeDBQ12QI6.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycSDEN318161:SDEN_1002-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_SHEDO
AccessionPrimary (citable) accession number: Q12QI6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: August 22, 2006
Last modified: January 25, 2012
This is version 44 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