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Q44052 (IMD_ARTGO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 74. 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:
Isomalto-dextranase

EC=3.2.1.94
Alternative name(s):
Exo-isomaltohydrolase
Glucan 1,6-alpha-isomaltosidase
Gene names
Name:imd
OrganismArthrobacter globiformis
Taxonomic identifier1665 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of (1->6)-alpha-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains.

Subcellular location

Secreted.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Sequence similarities

Belongs to the glycosyl hydrolase 27 family.

Contains 1 CBM6 (carbohydrate binding type-6) domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

glucan 1,6-alpha-isomaltosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939Tat-type signal
Chain40 – 641602Isomalto-dextranase
PRO_0000001022

Regions

Domain500 – 640141CBM6

Sites

Active site2271Nucleophile By similarity
Active site2881Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q44052 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B7F8F278F4D88350

FASTA64169,765
        10         20         30         40         50         60 
MMNLSRRTLL TTGSAATLAY ALGMAGSAQA ATAVTARPGV PVTAAPPLRL ASRNSVFTRS 

        70         80         90        100        110        120 
GAGPRYWNIY GYSFPHNAPI PENEWKANID WLAGNFADFG YDIACTDGWI EGSSRTTGNG 

       130        140        150        160        170        180 
YITSYNDSWQ HDWAYWANYL AARKMKLGVY YNPLWVHRAA VEDASKTVLG RPDVKIADLV 

       190        200        210        220        230        240 
VPGDFFARDI GGNQLYWLDV TKSGAKEYVQ GYVRYFKDLG VPYLRIDFLS WYEDGRDANI 

       250        260        270        280        290        300 
GQVNAPHGRA NYELALSWIN EAAGEDMEVS LVMPHMFQDG SAELANGDLV RINADADKGG 

       310        320        330        340        350        360 
WDRLSGMRQN WQDAWPNWAN PFCGFTGWSH RNGRGQLILD GDFMRASTFA SDEERKTMMN 

       370        380        390        400        410        420 
LMVAAGSPLA IADTYQQIGN NAWVYTNKEV LQLNADGLVG KPLYRSATPF SKDPGSRDTE 

       430        440        450        460        470        480 
RWAGQLPDGS WGVALFNRSD TETVTKTIDF AKDLGLATGG NVRDLWEHRN LGMDSRATAA 

       490        500        510        520        530        540 
LAPHASAIFR VTPPKMHGTT RYPAAFAAWG GGAGFNNNHP GYDGNGFVDG LQAGSGSADP 

       550        560        570        580        590        600 
LVTFAVQVPH RAATPSGYRY ANATDDNTTS KTTTKKANPE KADRSTVDGP VHVSFPGLAT 

       610        620        630        640 
WDTWGVAAGT ITLDAGLNLV TIGRGATDKG AINLNWIELD M 

« Hide

References

[1]"Molecular cloning and expression of an isomalto-dextranase gene from Arthrobacter globiformis T6."
Iwai A., Ito H., Mizuno T., Mori H., Matsui H., Honma M., Okada G., Chiba S.
J. Bacteriol. 176:7730-7734(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: T6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30761 Genomic DNA. Translation: BAA06424.1.
PIRA55549.

3D structure databases

ProteinModelPortalQ44052.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM35. Carbohydrate-Binding Module Family 35.
GH27. Glycoside Hydrolase Family 27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.70. 2 hits.
InterProIPR013785. Aldolase_TIM.
IPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR013780. Glyco_hydro_13_b.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
IPR006311. TAT_signal.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 2 hits.
PROSITEPS00512. ALPHA_GALACTOSIDASE. 1 hit.
PS51175. CBM6. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIMD_ARTGO
AccessionPrimary (citable) accession number: Q44052
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 74 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