DEXB_STRPN
ID DEXB_STRPN Reviewed; 535 AA.
AC Q54796; O07337; O54522; P96472; Q54514;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 135.
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; OrderedLocusNames=SP_0342;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-535.
RC STRAIN=406 / Type 3;
RX PubMed=8566758; DOI=10.1016/0378-1119(95)00657-5;
RA Arrecubieta C., Garcia E., Lopez R.;
RT "Sequence and transcriptional analysis of a DNA region involved in the
RT production of capsular polysaccharide in Streptococcus pneumoniae type 3.";
RL Gene 167:1-7(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-535.
RX PubMed=11902728; DOI=10.1046/j.1365-2958.1997.4341801.x;
RA Munoz R., Mollerach M.E., Lopez R., Garcia E.;
RT "Molecular organization of the genes required for the synthesis of type 1
RT capsular polysaccharide of Streptococcus pneumoniae: formation of binary
RT encapsulated pneumococci and identification of cryptic dTDP-rhamnose
RT biosynthesis genes.";
RL Mol. Microbiol. 25:79-92(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 375-535.
RC STRAIN=19F / SSZ;
RX PubMed=8021229; DOI=10.1128/jb.176.14.4437-4443.1994;
RA Morona J.K., Guidolin A., Morona R., Hansman D., Paton J.C.;
RT "Isolation, characterization, and nucleotide sequence of IS1202, an
RT insertion sequence of Streptococcus pneumoniae.";
RL J. Bacteriol. 176:4437-4443(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-535.
RC STRAIN=SP-VA92 / Serotype 19F, and SP-VA96;
RX PubMed=9466257; DOI=10.1046/j.1365-2958.1998.00658.x;
RA Coffey T.J., Enright M.C., Daniels M., Morona J.K., Morona R.,
RA Hryniewicz W., Paton J.C., Spratt B.G.;
RT "Recombinational exchanges at the capsular polysaccharide biosynthetic
RT locus lead to frequent serotype changes among natural isolates of
RT Streptococcus pneumoniae.";
RL Mol. Microbiol. 27:73-83(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 420-535.
RC STRAIN=NCTC 11902 / Serotype 14;
RX PubMed=9383201; DOI=10.1046/j.1365-2958.1997.5791940.x;
RA Kolkman M.A.B., Wakarchuk W., Nuijten P.J.M., van der Zeijst B.A.M.;
RT "Capsular polysaccharide synthesis in Streptococcus pneumoniae serotype 14:
RT molecular analysis of the complete cps locus and identification of genes
RT encoding glycosyltransferases required for the biosynthesis of the
RT tetrasaccharide subunit.";
RL Mol. Microbiol. 26:197-208(1997).
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; AE005672; AAK74516.1; -; Genomic_DNA.
DR EMBL; Z47210; CAA87400.1; -; Genomic_DNA.
DR EMBL; Z83335; CAB05933.1; -; Genomic_DNA.
DR EMBL; U04047; AAA21853.1; -; Genomic_DNA.
DR EMBL; AF030367; AAC38714.1; -; Genomic_DNA.
DR EMBL; AF030368; AAC38720.1; -; Genomic_DNA.
DR EMBL; AF030369; AAC38725.1; -; Genomic_DNA.
DR EMBL; AF030370; AAC38729.1; -; Genomic_DNA.
DR EMBL; AF030371; AAC38734.1; -; Genomic_DNA.
DR EMBL; AF030372; AAC38739.1; -; Genomic_DNA.
DR EMBL; AF030374; AAC38763.1; -; Genomic_DNA.
DR EMBL; X85787; CAA59784.1; -; Genomic_DNA.
DR PIR; C95040; C95040.
DR PIR; T50029; T50029.
DR RefSeq; WP_001156825.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q54796; -.
DR SMR; Q54796; -.
DR STRING; 170187.SP_0342; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q54796; -.
DR EnsemblBacteria; AAK74516; AAK74516; SP_0342.
DR KEGG; spn:SP_0342; -.
DR eggNOG; COG0366; Bacteria.
DR OMA; RDWYWWR; -.
DR PhylomeDB; Q54796; -.
DR BioCyc; SPNE170187:G1FZB-351-MON; -.
DR Proteomes; UP000000585; Chromosome.
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; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycosidase; Hydrolase.
FT CHAIN 1..535
FT /note="Glucan 1,6-alpha-glucosidase"
FT /id="PRO_0000054340"
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"
FT VARIANT 461
FT /note="V -> I (in strain: 406 / Type 3, 19F and SP-VA96)"
FT CONFLICT 375..381
FT /note="YAREALE -> MRVRLLK (in Ref. 4; AAA21853)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="A -> P (in Ref. 2; CAA87400)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="G -> D (in Ref. 5; AAC38725/AAC38739)"
FT /evidence="ECO:0000305"
FT CONFLICT 514..519
FT /note="AAKEVL -> LAQEVF (in Ref. 2; CAA87400, 3; CAB05933,
FT 4; AAA21853 and 5; AAC38714/AAC38720/AAC38725/AAC38729/
FT AAC38734/AAC38739/AAC38763)"
FT /evidence="ECO:0000305"
FT CONFLICT 523..525
FT /note="VLA -> ILV (in Ref. 2; CAA87400, 3; CAB05933, 4;
FT AAA21853 and 5; AAC38714/AAC38720/AAC38725/AAC38729/
FT AAC38734/AAC38739/AAC38763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 62035 MW; AD78F733204DA944 CRC64;
MQEKWWHNAV VYQVYPKSFM DSNGDGVGDL PGITSKLDYL AKLGITAIWL SPVYDSPMDD
NGYDIADYQA IAAIFGTMED MDQLIAEAKK RDIRIIMDLV VNHTSDEHAW FVEACENTDS
PERDYYIWRD EPNDLDSIFS GSAWEYDEKS GQYYLHFFSK KQPDLNWENE KLRQKIYEMM
NFWIDKGIGG FRMDVIDMIG KIPDEKVVNN GPMLHPYLKE MNQATFGDKD LLTVGETWGA
TPEIAKFYSD PKGQELSMVF QFEHIGLQYQ EGQPKWHYQK ELNIAKLKEI FNKWQTELGV
EDGWNSLFWN NHDLPRIVSI WGNDQEYREK SAKAFAILLH LMRGTPYIYQ GEEIGMTNYP
FETLDQVEDI ESLNYAREAL EKGVPIEEIM DSIRVIGRDN ARTPMQWDES KNAGFSTGQP
WLAVNPNYEM INVQEALANP DSIFYTYQKL VQIRKENSWL VRADFELLDT ADKVFAYIRK
DGDRRFLVVA NLSNEEQDLT VEGKVKSVLI ENTAAKEVLE KQVLAPWDAF CVELL
