DEXT_BACLI
ID DEXT_BACLI Reviewed; 10 AA.
AC C0HJE3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 02-JUN-2021, entry version 6.
DE RecName: Full=Dextranase {ECO:0000303|Ref.1};
DE EC=3.2.1.11 {ECO:0000269|Ref.1};
DE AltName: Full=Alpha-1,6-glucan-6-glucanohydrolase {ECO:0000250|UniProtKB:P39653};
DE Flags: Fragment;
OS Bacillus licheniformis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=KIBGE-IB25 {ECO:0000269|Ref.1};
RA Zohra R.R., Sattar H., Karim A., Aman A., Qader S.A.;
RT "Dextranase: isolation, purification and characterization of dextran
RT degrading enzyme from Bacillus licheniformis KIBGE-IB25.";
RL Submitted (AUG-2013) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in
CC dextran.; EC=3.2.1.11; Evidence={ECO:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Because of the indeterminate molecular weight of dextran, an
CC approximate KM value of 0.3738 mg/ml was determined.
CC {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 4.5,
CC its MW is: 158 kDa. {ECO:0000269|Ref.1}.
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DR BRENDA; 3.2.1.11; 669.
DR GO; GO:0033904; F:dextranase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation.
FT CHAIN 1..>10
FT /note="Dextranase"
FT /id="PRO_0000424175"
FT NON_TER 10
FT /evidence="ECO:0000303|Ref.1"
SQ SEQUENCE 10 AA; 1128 MW; 924BD23B5731B2D1 CRC64;
AYTVTLYLQG