ID A0A1H4JD39_9FLAO Unreviewed; 763 AA.
AC A0A1H4JD39;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=SAMN04489761_0734 {ECO:0000313|EMBL:SEB44121.1};
OS Tenacibaculum sp. MAR_2009_124.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1250059 {ECO:0000313|EMBL:SEB44121.1, ECO:0000313|Proteomes:UP000199366};
RN [1] {ECO:0000313|EMBL:SEB44121.1, ECO:0000313|Proteomes:UP000199366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2009_124 {ECO:0000313|EMBL:SEB44121.1,
RC ECO:0000313|Proteomes:UP000199366};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR EMBL; FNSF01000001; SEB44121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4JD39; -.
DR STRING; 1250059.SAMN04489761_0734; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000199366; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000199366}.
FT DOMAIN 683..752
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 763 AA; 84214 MW; 6A276CE7DC49FE08 CRC64;
MRKSLLVIII IAFNSCNKTN SEAKISDSMN STVVNNSIEQ KIDSLLEIMT LEEKVGQMNQ
YNGFWDATGP VPKKGSQAEK YADLKKGLVG SMLNVRGVKQ VKALQQIAVE ETRLGIPLIF
GFDVIHGFKT ITPVPLAEAA SWDLNIIEKS AKNAAEEAAV AGLNWTFAPM IDIYRDARWG
RVMEGGGEDP YLGSKIAVAR VKGFQGDDLS SSKTIAACAK HFAAYGFIES GREYNTVDIG
TSTLYNTVLP PFKEVADAGV KTFMNAFNEL NGIPATADTF LQREVLKKDW NFKGFVISDW
GSIGELVAHG YAKDLKQATE LAVKAGSDMD MESSAYVEEL AGLVKEGAVN EKLINDAVRR
ILRVKYELGL FDDPYRYCDE KKEQEITGKK QFHEDALDIA KKSIVLLKND NNILPLKKQG
IKVAIIGALA NDKTSPLGNW RLAAKEGTAI SVVEGFRKYS GNELQYAKGA DLVIPNTEIS
MTQEVQVNTT NTSEFGEALS LAKKSDVVVM VLGEHGMQSG EARSRSTIDL PGVQQQLLEE
VYKVNEKIVL VLMNGRPLAF PWAKENIPGI IEGWQLGVES GNAIAQVVYG DYNPSGKLPM
TFPKSLGQVP LYYNYKNTGR PVRDGNVFWS HYSDETNDPL YPFGYGLSYT SFSYENLNVE
IVDTHEVMVS VDVMNTGKVK GKEVVQLYIH DEYASVTRPV RELKGFEMIA IESGKSKKVE
FKLTEKELGF YNNKGEFLVE PGKFSVFVGG DSKAELTNTF TLK
//
