ID A0A223NUK3_9SPHI Unreviewed; 725 AA.
AC A0A223NUK3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=MuYL_1657 {ECO:0000313|EMBL:ASU33553.1};
OS Mucilaginibacter xinganensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1234841 {ECO:0000313|EMBL:ASU33553.1, ECO:0000313|Proteomes:UP000215002};
RN [1] {ECO:0000313|EMBL:ASU33553.1, ECO:0000313|Proteomes:UP000215002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJC16-A31 {ECO:0000313|EMBL:ASU33553.1,
RC ECO:0000313|Proteomes:UP000215002};
RG Henan University of Science and Technology;
RA You X.;
RT "Complete genome sequence of Mucilaginibacter sp. strain BJC16-A31.";
RL Submitted (AUG-2017) 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; CP022743; ASU33553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223NUK3; -.
DR KEGG; muc:MuYL_1657; -.
DR Proteomes; UP000215002; Chromosome.
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:UP000215002}.
FT DOMAIN 644..713
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 725 AA; 78508 MW; 02C298719D2DF493 CRC64;
MGKMTLDEKI GQLNLVVMGN AITGTVISKG VEDKMKRGEI GGIFGLYGTA NVSKMQDLAV
KQSRLHIPLI FGLDVIHGHR TIFPIPLGVS ATWDMGLIQQ SAKIAAKEAT AEGLNWVFSP
MVDIARDPRW GRISEGSGED PWYGSKVAKA MVKGYQGNNL MDADAVMACV KHFALYGGAE
AGREYNTVDM SLIKMYQDYL PPYKAAVDAG AGSFMSSFNT INGMPATVNK WLLTDLLRKQ
WGFKGFVVSD YTALNEVTNH GLGDLQTVSA LALKAGLDMD MVGEGFLTTL KKSLKEGKVT
PQEIDLACRR VLEAKYKLGL FKNPAKSINA EKEKQDVFTD DNRKFARQIA EHSFVLLKNQ
GETLPLKKSG TIALVGPLAD NHSEMLGTWV IAGDPNKSVS VAEGIKNVVG ENVKVLYAKG
ANITDDSLLS IRAFALTGPE VKDKRTPQEM IDEAVETAKK ADVVVAVVGE SANMSGESSS
RADIDIPESQ KELLKALSKT GKPLVIVLFN GRPLTLTWED KHASAILDAW APGTEAGNAI
ADVLFGNYNP AGKLTATFPR SVGQIPIYYS HKNTGRPFDG TGGAKFKSDY LDISNDPLYP
FGYGLSYTTF SYSGVQLDKT NPAGNTTVKA TVTVTNTGKY AGEEVVQLYI SDPVASISRS
VKELKGFQKI SLQPGESKVV SFNITTADLK FYNDKLIYDW EPGQFVVQIG TNSANVQSAA
VQWLK
//
