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P39652 (DEXT_ARTSD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dextranase
EC=3.2.1.11
Alternative name(s):
Alpha-1,6-glucan-6-glucanohydrolase
Endodextranase
OrganismArthrobacter sp. (strain CB-8)
Taxonomic identifier74565 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length640 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Efficiently decomposes water-insoluble glucan as well as dextran.

Catalytic activity

Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in dextran.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 49 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0.

Temperature dependence:

Optimum temperature is 42 degrees Celsius.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondextranase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Propeptide33 – 4917
PRO_0000012211
Chain50 – 640591Dextranase
PRO_0000012212

Sequences

Sequence LengthMass (Da)Tools
P39652 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: E9D9833A203602B6

FASTA64071,289
        10         20         30         40         50         60 
MPGTGLGRLA KRMTAAAAVF FISTSAVLPA QAATAPAAAP PGVPAALKAE RAITTVDNGN 

        70         80         90        100        110        120 
LHTWWHDNGV FSPATPTQSS EVRRSSFYDV QVAQANQPQK LYDAFSYMSI PRSGKGKIGY 

       130        140        150        160        170        180 
TEEDGAEFSS DARLTMSWSS FEYAKDVWVE VSLRTGQTIS SADQVQIRPS SYNFEKQLVD 

       190        200        210        220        230        240 
ADTVRIKVPY SDAGYRFSVE FEPQLYTAYN DMSGDSGKLT TEAAGNRPIH TEPRNSMMVF 

       250        260        270        280        290        300 
AEPKLRGEQK ERLVPTEESG SIHYPEPGEV RNLNSVSEEI IYFRPGTYSM GPDYHAVLPA 

       310        320        330        340        350        360 
NVKWVYLAPG AYVKGAFRFL HDTQSQYKVT GYGVLSGEQY VYEADTNNSY HHLSGASNCH 

       370        380        390        400        410        420 
SSCVKMLQFA SADAEQKLDL QGVTVAEPPY HSFVVYGNEQ TFHMNVENYK QVGSWYWQTD 

       430        440        450        460        470        480 
GIELYKGSTM KNTFFNANDD VLKMYHSDVT IDNTVIWKNE NGPVIQWGWT PRNIDNVNVA 

       490        500        510        520        530        540 
NTTVIHNRMY WKDVKYNTCI FNSSSHWEDM GSTTKADPNT TVKNMRFENT AVEGMTNCAI 

       550        560        570        580        590        600 
RVYALSDTEN IHIKNFNIGA WNGLEWTSQV SHLKRYTNSA GEKVTIGNEV PDGNGLALEN 

       610        620        630        640 
YSVGGQVIEK TGGNSSDYQL GRLGFDGENW ENWNAWKSAP

« Hide

References

[1]"Molecular cloning and nucleotide sequencing of the Arthrobacter dextranase gene and its expression in Escherichia coli and Streptococcus sanguis."
Okushima M., Sugino D., Kouno Y., Nakano S., Miyahara J., Toda H., Kubo S., Matsushiro A.
Jpn. J. Genet. 66:173-187(1991) [PubMed: 1859672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 50-61.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D00834 Genomic DNA. Translation: BAA00708.1.

3D structure databases

ProteinModelPortalP39652.
ModBaseSearch...

Protein family/group databases

CAZyGH49. Glycoside Hydrolase Family 49.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005192. Glyco_hydro_49.
IPR023226. Glyco_hydro_49_N_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
Gene3DG3DSA:2.60.350.10. Glyco_hydro_49_N. 1 hit.
G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF03718. Glyco_hydro_49. 1 hit.
[Graphical view]
SUPFAMSSF101596. Glyco_hydro_49_N. 1 hit.
SSF51126. Pectin_lyas_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEXT_ARTSD
AccessionPrimary (citable) accession number: P39652
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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