ID H2ITQ9_RAHAC Unreviewed; 765 AA.
AC H2ITQ9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN OrderedLocusNames=Rahaq2_0584 {ECO:0000313|EMBL:AEX50511.1};
OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS NCIMB 13365 / CIP 78.65).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Rahnella.
OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX50511.1, ECO:0000313|Proteomes:UP000009010};
RN [1] {ECO:0000313|EMBL:AEX50511.1, ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RX PubMed=22582378; DOI=10.1128/JB.00380-12;
RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA Tapia R., Woyke T., Sobecky P.A.;
RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL J. Bacteriol. 194:3020-3021(2012).
RN [2] {ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA Martinez R., Woyke T.;
RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL Submitted (JAN-2012) 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; CP003244; AEX50511.1; -; Genomic_DNA.
DR RefSeq; WP_014333768.1; NZ_JMPO01000134.1.
DR AlphaFoldDB; H2ITQ9; -.
DR STRING; 745277.Rahaq2_0584; -.
DR GeneID; 61510718; -.
DR KEGG; raq:Rahaq2_0584; -.
DR PATRIC; fig|745277.3.peg.553; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_6; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000009010; 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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000009010};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..765
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003562777"
FT DOMAIN 685..754
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 765 AA; 83531 MW; 243B1032A1C811DC CRC64;
MNTHHMLGAL VLLVSSASSL AVETTGIPQD QVKERNAFIA DLMKKMTLDE KIGQLNLVTV
GPEYQKEAIM ADIRAGKVGG VFNTVTKPDI RRMQDQVQYS RLKIPPFYAY DVVHGQRTIF
PISLGLAASW DMQAVATSAR ISALETAADG LNMTFSPMVD ITRDPRWGRV SEGFGEDTYL
TSRLAHEMVT GYQGKDPSAP DAVMANVKHY ALYGAVEGGR EYNTVDMSLT RMFNDYMPPY
KAAVDAGAGG VMVALNSING IPATSNTWLL KDILRDDWQF KGLTVSDHGA IGGLVKHGVA
EDDRQAAAMA LKAGVDMDMA DNMYGKYLKG LLADGLVSQK DIDRAVRDVL AAKWDMGLFV
DEYRHLGPPS SDPADTNAES RLHRQEAREV ARTSLVLLKN NDQTLPLQKK GTIAVVGALA
DSKRDVMGSW SAAGKAAQAV TVLQGMKDVL GDKGTILYAR GANVTDDQAM VDFLNSYEKQ
VINDPRKPQD MIDEAVKTAE KADVVVAVVG EAQGMAHEAS SRSDINIPQS QRDLLKALKA
TGKPLVVVLM NGRPLTLSWE NEISDAMLET WFSGTEGGHA IADVLFGDYN PSGKLPMTFP
RSVGQIPLYN SVLNTGRPFN PQHPDKYTTR YFDITNGPLF PFGYGLSYTR FSVSDVNLSS
TTMDAGHPLT ASVTVKNTGK VSGATIVQMY LQDVTASISR PVKELKNFEK INLQPGEEKI
VTFAITEKDL RFYNDKLKWA SEPGKFNVFV GLDSQDVKKT SFLLK
//
