ID   DEXB_STREQ              Reviewed;         537 AA.
AC   Q59905;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Glucan 1,6-alpha-glucosidase;
DE            EC=3.2.1.70;
DE   AltName: Full=Dextran glucosidase;
DE   AltName: Full=Exo-1,6-alpha-glucosidase;
DE   AltName: Full=Glucodextranase;
GN   Name=dexB;
OS   Streptococcus dysgalactiae subsp. equisimilis (Streptococcus equisimilis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=119602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H46A;
RX   PubMed=8232196; DOI=10.1007/bf00280210;
RA   Mechold U., Steiner K., Vettermann S., Malke H.;
RT   "Genetic organization of the streptokinase region of the Streptococcus
RT   equisimilis H46A chromosome.";
RL   Mol. Gen. Genet. 241:129-140(1993).
CC   -!- FUNCTION: The physiological substrates may be short
CC       isomaltosaccharides. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in (1->6)-
CC         alpha-D-glucans and derived oligosaccharides.; EC=3.2.1.70;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X72832; CAA51348.1; -; Genomic_DNA.
DR   PIR; S39970; S39970.
DR   AlphaFoldDB; Q59905; -.
DR   SMR; Q59905; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043896; F:glucan 1,6-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.90.400.10; -; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosidase; Hydrolase.
FT   CHAIN           1..537
FT                   /note="Glucan 1,6-alpha-glucosidase"
FT                   /id="PRO_0000054338"
FT   ACT_SITE        194
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        236
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            313
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   537 AA;  61733 MW;  154DF0ACAF302FC7 CRC64;
     MQKQWWHKAT IYQIYPRSFK DTSGNGIGDL KGITSQLDYL QKLGITAIWL SPVYQSPMDD
     NGYDISDYEA IAEVFGNMDD MDDLLAAANE RGIKIIMDLV VNHTSDEHAW FVEARENPNS
     PERDYYIWRD EPNNLMSIFS GSAWELDEAS GQYYLHLFSK KQPDLNWENA HVRQKIYDMM
     NFWIAKGIGG FRMDVIDLIG KIPDSEITGN GPRLHDYLKE MNQATFGNHD VMTVGETWGA
     TPEIARQYSR PENKELSMVF QFEHVGLQHK PNAPKWDYAE ELDVPALKTI FSKWQTELKL
     GEGWNSLFWN NHDLPRVLSI WGNDSIYREK SAKALAILLH LMRGTPYIYQ GEEIGMTNYP
     FKDLTEVDDI ESLNYAKEAM ENGVPAARVM SSIRKVGRDN ARTPMQWSKD THAGFSEAQE
     TWLPVNPNYQ EINVADALAN QDSIFYTYQQ LIALRKDQDW LVEADYHLLP TADKVFAYQR
     QFGEETYVIV VNVSDQEQVF AKDLAGAEVV ITNTDVDKVL ETKHLQPWDA FCVKLSV