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Reviewed, UniProtKB/Swiss-Prot A1S457 (GLMM1_SHEAM)

Last modified November 3, 2009. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoglucosamine mutase 1
    EC=5.4.2.10
Gene names
Name: glmM1
Ordered Locus Names: Sama_0956
OrganismShewanella amazonensis (strain ATCC BAA-1098 / SB2B) [Complete proteome] [HAMAP]
Taxonomic identifier326297 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity.

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP 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: UniProtKB-KW

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Phosphoglucosamine mutase 1 HAMAP MF_01554
PRO_0000305670

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
A1S457-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 7D253F79A71BB67E

FASTA44547,764
        10         20         30         40         50         60 
MSQRKFFGTD GIRGKVGADQ MTPELALKLG WAAGRVLART GTKKVIIGKD TRISGYMFES 

        70         80         90        100        110        120 
ALEAGFSSAG LNVLLMGPMP TPAVAYLTRT FRAEAGVVIS ASHNPYYDNG IKFFSNDGSK 

       130        140        150        160        170        180 
LDDEIELAIE AELEKPLICA ESQFLGKVSR IDDARGRYIE YCKGNFPADQ TLSGLKIVVD 

       190        200        210        220        230        240 
CAHGATYHIA PAVFRELGAE VVAIGVEPNG MNINDKCGAT SMGAIRDKVL EVNADLGIAL 

       250        260        270        280        290        300 
DGDGDRIMMV TQEGDIIDGD QILYILALDA KERGLLKGGV VGTQMANLGL ELALKDEGIP 

       310        320        330        340        350        360 
FARSKVGDRY VMELLKELGW RIGGENSGHI LNLDHGTTGD GIVAGILVLA AMRRSGKGLQ 

       370        380        390        400        410        420 
QLIAKLKMFP QVLVNVRFEG DKNPLEADTV TAKVAEVERE LGERGRVLLR KSGTEPLLRV 

       430        440 
MVEGEDKETV TRLANAIADA VKAAT 

« Hide

References

[1]"Complete sequence of Shewanella amazonensis SB2B."
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000507 Genomic DNA. Translation: ABL99163.1.
RefSeqYP_926833.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1S457.

Genome annotation databases

GeneID4603208.
GenomeReviewsGene locus Sama_0956 in contig CP000507_GR.
KEGGsaz:Sama_0956.
NMPDRfig|326297.7.peg.897.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAEPMKMLP.

Family and domain databases

HAMAPMF_01554.
[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. A-D-PHexomutase_N.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM1_SHEAM
AccessionPrimary (citable) accession number: A1S457
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents