Reviewed, UniProtKB/Swiss-Prot P39652 (DEXT_ARTSD)

Names and origin

Protein names	Recommended name:     Dextranase     EC=3.2.1.11 Alternative name(s):     Alpha-1,6-glucan-6-glucanohydrolase     Endodextranase
Organism	Arthrobacter sp. (strain CB-8)
Taxonomic identifier	74565 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	640 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dextranase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 32	32	Potential
	Propeptide	33 – 49	17	Ref.1		PRO_0000012211
	Chain	50 – 640	591	Dextranase		PRO_0000012212

Sequences

	Sequence		Length	Mass (Da)
	P39652-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: E9D9833A203602B6	FASTA	640	71,289
	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

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
EMBLGenBankDDBJ	D00834 Genomic DNA. Translation: BAA00708.1.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH49. Glycoside Hydrolase Family 49.
Family and domain databases
InterPro	IPR005192. Glyco_hydro_49. IPR012334. Pectin_lyas_fold. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
Pfam	PF03718. Glyco_hydro_49. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DEXT_ARTSD

Accession

Primary (citable) accession number: P39652

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)