DEXB_STRMU
ID DEXB_STRMU Reviewed; 536 AA.
AC Q99040;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
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=SMU_883;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ingbritt;
RX PubMed=2380687; DOI=10.1099/00221287-136-5-803;
RA Russell R.R.B., Ferretti J.J.;
RT "Nucleotide sequence of the dextran glucosidase (dexB) gene of
RT Streptococcus mutans.";
RL J. Gen. Microbiol. 136:803-810(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: The physiological substrates may be short
CC isomaltosaccharides.
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.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; M77351; AAA26939.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58598.1; -; Genomic_DNA.
DR PIR; A37231; A37231.
DR RefSeq; NP_721292.1; NC_004350.2.
DR RefSeq; WP_002262877.1; NC_004350.2.
DR PDB; 2ZIC; X-ray; 2.20 A; A=1-536.
DR PDB; 2ZID; X-ray; 2.20 A; A=1-536.
DR PDB; 4WLC; X-ray; 2.40 A; A=1-536.
DR PDB; 4XB3; X-ray; 2.09 A; A=1-536.
DR PDBsum; 2ZIC; -.
DR PDBsum; 2ZID; -.
DR PDBsum; 4WLC; -.
DR PDBsum; 4XB3; -.
DR AlphaFoldDB; Q99040; -.
DR SMR; Q99040; -.
DR STRING; 210007.SMU_883; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q99040; -.
DR EnsemblBacteria; AAN58598; AAN58598; SMU_883.
DR KEGG; smu:SMU_883; -.
DR PATRIC; fig|210007.7.peg.789; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_1_2_9; -.
DR OMA; RDWYWWR; -.
DR PhylomeDB; Q99040; -.
DR BRENDA; 3.2.1.70; 5941.
DR SABIO-RK; Q99040; -.
DR EvolutionaryTrace; Q99040; -.
DR Proteomes; UP000002512; 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; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..536
FT /note="Glucan 1,6-alpha-glucosidase"
FT /id="PRO_0000054339"
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 CONFLICT 72
FT /note="T -> A (in Ref. 1; AAA26939)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="G -> D (in Ref. 1; AAA26939)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="A -> T (in Ref. 1; AAA26939)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="V -> I (in Ref. 1; AAA26939)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:4XB3"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4XB3"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:4XB3"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:4XB3"
FT TURN 225..230
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 242..249
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 284..297
FT /evidence="ECO:0007829|PDB:4XB3"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 370..380
FT /evidence="ECO:0007829|PDB:4XB3"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 386..396
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 434..439
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 444..457
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:2ZID"
FT STRAND 475..482
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 485..492
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 506..514
FT /evidence="ECO:0007829|PDB:4XB3"
FT HELIX 516..522
FT /evidence="ECO:0007829|PDB:4XB3"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:4WLC"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:4XB3"
SQ SEQUENCE 536 AA; 62030 MW; F3287CD6C8DBD8D2 CRC64;
MQKHWWHKAT VYQIYPKSFM DTNGDGIGDL KGITSKLDYL QKLGVMAIWL SPVYDSPMDD
NGYDIANYEA ITDIFGNMAD MDNLLTQAKM RGIKIIMDLV VNHTSDEHAW FIEAREHPDS
SERDYYIWCD QPNDLESIFG GSAWQYDDKS DQYYLHFFSK KQPDLNWENA NLRQKIYDMM
NFWIDKGIGG FRMDVIDMIG KIPAQHIVSN GPKLHAYLKE MNAASFGQHD LLTVGETWGA
TPEIAKQYSN PVNHELSMVF QFEHIGLQHK PEAPKWDYVK ELNVPALKTI FNKWQTELEL
GQGWNSLFWN NHDLPRVLSI WGNTGKYREK SAKALAILLH LMRGTPYIYQ GEEIGMTNYP
FKDLNELDDI ESLNYAKEAF TNGKSMETIM DSIRMIGRDN ARTPMQWDAS QNAGFSTADK
TWLPVNPNYK DINVQAALKN SNSIFYTYQQ LIQLRKENDW LVDADFELLP TADKVFAYLR
KVREERYLIV VNVSDQEEVL EIDVDKQETL ISNTNESAAL ANHKLQPWDA FCIKIN
