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A3D6B7 (GH109_SHEB5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Glycosyl hydrolase family 109 protein

EC=3.2.1.-
Gene names
Ordered Locus Names:Sbal_2793
OrganismShewanella baltica (strain OS155 / ATCC BAA-1091) [Complete proteome] [HAMAP]
Taxonomic identifier325240 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Glycosidase By similarity.

Cofactor

Binds 1 NAD+ per subunit. The NAD cannot dissociate By similarity.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Sequence similarities

Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109 subfamily.

Ontologies

Keywords
   DomainSignal
   LigandNAD
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular_functionhydrolase activity, acting on glycosyl bonds

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131Tat-type signal Potential
Chain32 – 459428Glycosyl hydrolase family 109 protein
PRO_5000224660

Regions

Nucleotide binding64 – 652NAD By similarity
Nucleotide binding135 – 1384NAD By similarity
Nucleotide binding155 – 1562NAD By similarity
Region244 – 2474Substrate binding By similarity

Sites

Binding site861NAD By similarity
Binding site1841NAD By similarity
Binding site2131Substrate By similarity
Binding site2321Substrate By similarity
Binding site2441NAD By similarity
Binding site3261Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A3D6B7 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 73B38A8DE6ADDFAA

FASTA45951,893
        10         20         30         40         50         60 
MHNIHRRNFL KAAGAATAGL VTANIALNAY ASSVAPKPQA GKSVIGLIAP KMDVVRVGFI 

        70         80         90        100        110        120 
GVGERGFSHV EQFCHLEGVE LKAICDTHQA VLDRAVDHIV KQNRPKPAVY TGNDLSYRDL 

       130        140        150        160        170        180 
LSRDDIDIVI ISTPWEWHAP MAIETMESGK HAFVEVPMAL TVEECWQVVD TAERTQKNCM 

       190        200        210        220        230        240 
MMENVNYGRE ELMVLNMVRQ GVFGELLHGE AAYIHELRWQ MKEIDHKTGS WRTYWHTKRN 

       250        260        270        280        290        300 
GNLYPTHGLG PVSQYMNINR GDRFDYLTSM SSPALGRALY AKREFPADHE RNQLKYINGD 

       310        320        330        340        350        360 
INTSLIKTVK GRTIMVQHDT TTPRPYSRHN LIQGTNGVFA GFPNRIAVEN GGFGQSYHEW 

       370        380        390        400        410        420 
DMDMQKWYDK YDHPLWQRIG KEAEINGGHG GMDFVMLWRM IYCLRNGEAL DQDVYDGASW 

       430        440        450 
SVVNILSEHS LNDRSNSVTF PDFTRGAWQT AKPLGIVGA 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS155."
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., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I., Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS155 / ATCC BAA-1091.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000563 Genomic DNA. Translation: ABN62280.1.
RefSeqYP_001051149.1. NC_009052.1.

3D structure databases

ProteinModelPortalA3D6B7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING325240.Sbal_2793.

Protein family/group databases

CAZyGH109. Glycoside Hydrolase Family 109.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN62280; ABN62280; Sbal_2793.
GeneID4842508.
KEGGsbl:Sbal_2793.
PATRIC37184670. VBISheBal55297_3140.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG125103.
HOGENOMHOG000252553.
OMAHNIHRRH.
OrthoDBEOG61P6MK.

Enzyme and pathway databases

BioCycSBAL325240:GCTA-2864-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
IPR006311. TAT_signal.
IPR019546. TAT_signal_bac_arc.
[Graphical view]
PfamPF01408. GFO_IDH_MocA. 1 hit.
PF10518. TAT_signal. 1 hit.
[Graphical view]
TIGRFAMsTIGR01409. TAT_signal_seq. 1 hit.
PROSITEPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGH109_SHEB5
AccessionPrimary (citable) accession number: A3D6B7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 46 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries