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Database: UniProt
Entry: D2Q7E5_BIFDB
LinkDB: D2Q7E5_BIFDB
Original site: D2Q7E5_BIFDB 
ID   D2Q7E5_BIFDB            Unreviewed;       676 AA.
AC   D2Q7E5;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=AglL Glycosyl hydrolases family 31, Alpha-glucosidase {ECO:0000313|EMBL:ADB10707.1};
DE            EC=3.2.1.3 {ECO:0000313|EMBL:ADB10707.1};
GN   Name=aglL {ECO:0000313|EMBL:ADB10707.1};
GN   OrderedLocusNames=BDP_2149 {ECO:0000313|EMBL:ADB10707.1};
OS   Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB10707.1, ECO:0000313|Proteomes:UP000008693};
RN   [1] {ECO:0000313|EMBL:ADB10707.1, ECO:0000313|Proteomes:UP000008693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC   {ECO:0000313|Proteomes:UP000008693};
RX   PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA   Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA   Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA   Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA   Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT   "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT   adaptation to the human oral cavity.";
RL   PLoS Genet. 5:E1000785-E1000785(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; CP001750; ADB10707.1; -; Genomic_DNA.
DR   RefSeq; WP_003838285.1; NC_013714.1.
DR   AlphaFoldDB; D2Q7E5; -.
DR   STRING; 401473.BDP_2149; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   GeneID; 69535739; -.
DR   KEGG; bde:BDP_2149; -.
DR   eggNOG; COG1501; Bacteria.
DR   HOGENOM; CLU_000631_10_0_11; -.
DR   Proteomes; UP000008693; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd14752; GH31_N; 1.
DR   CDD; cd06593; GH31_xylosidase_YicI; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR   PANTHER; PTHR43053:SF4; RE74917P; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:ADB10707.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:ADB10707.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008693}.
FT   DOMAIN          55..218
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          261..575
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          584..671
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
SQ   SEQUENCE   676 AA;  76555 MW;  934EB04227B6285C CRC64;
     MKFLNGGWLV KDGFSVKYAA NIYTANIEPK KLTLFCPFGS PIYNAGMTLD GGILTIEVTS
     PREDVITTKL INFKKDRSNC PKFGLNETDP DVEIDETDDK WTFTSGRLTL EIAKGETIDF
     KYLYDGKVIA HSGWRAKGLV TDPEGQLHVS EQLDLGVGEK IYGLGERFTN FIKNGQTVDI
     WNEDGGTGTE QAYKNIPFYL SNRKYGLFVD NPGKVSFEVG SEKVSRVQFS VPGEEMSYSV
     VGGENLKAIL NTYTDLTGKA PLVPDWSYGL WLSTSFTTDY DEKTVLEFVD GMAERNIPLS
     VFHFDCRWMK ELEWCNFDWD KSKFPDPEGL LKKLHDRGLK ICVWINSYIG QKSPLFEEGA
     KNGYFIKNED GSVWQWDRWQ AGMAIVDFTN PEATKWYQGY LKKLVAMGVD CFKTDFGERI
     PTEGVKYYDG SDPELMHNYY TYLYNKAVYD VLVETKGADE AILFARSATV GGQQFPVHWG
     GDCSSNYPSM AESLRAGLSF GMSGFGYWSH DIAGFEDQAS PDLYKRWTQF GLLSSHSRYH
     GSTAYKVPWL YGDEAVDVAR EFTELKLQLK PYLLKMAQET HETGVPMMRA MVLEFPDDPT
     CEDIDTQYML GDDLLVAPVF REDGVARFYV PDDGTGQAWT NIITDTAYEP GKWYTEQYDY
     HTLPVLARPG TDPLHV
//
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