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Database: UniProt
Entry: A9DI37_9FLAO
LinkDB: A9DI37_9FLAO
Original site: A9DI37_9FLAO 
ID   A9DI37_9FLAO            Unreviewed;       404 AA.
AC   A9DI37;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=KAOT1_11487 {ECO:0000313|EMBL:EDP97833.1};
OS   Kordia algicida OT-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kordia.
OX   NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP97833.1, ECO:0000313|Proteomes:UP000002945};
RN   [1] {ECO:0000313|EMBL:EDP97833.1, ECO:0000313|Proteomes:UP000002945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT-1 {ECO:0000313|EMBL:EDP97833.1,
RC   ECO:0000313|Proteomes:UP000002945};
RX   PubMed=21622754; DOI=10.1128/JB.05241-11;
RA   Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT   "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL   J. Bacteriol. 193:4031-4032(2011).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP97833.1}.
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DR   EMBL; ABIB01000001; EDP97833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9DI37; -.
DR   STRING; 391587.KAOT1_11487; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_12_0_10; -.
DR   Proteomes; UP000002945; 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; 2.
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   PANTHER; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EDP97833.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002945}.
FT   DOMAIN          55..274
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
SQ   SEQUENCE   404 AA;  44355 MW;  269F10A515F582CF CRC64;
     MNSKYHKVFI IASIGIFLLG CVTNKKNGSQ MEVVKETSKK TPVDKRVDSL LAKMTLDEKV
     GQMNLYNGFW DVTGPTPKEG NAKLKYDHLK KGWVGAMLNV RGTKNVYEVQ RIAVEETRLG
     IPLLIGFDVI HGYKTLSPIP LAESSSWDLD AIKSSARVAA IEASSAGINW TFAPMVDISR
     DPRWGRVMEG GGEDPYLGSK IASARVHGFQ GDDLTNQHSI AACAKHFAAY GFAEAGKEYN
     TVDIGTSTLY NTVLPPFKAA ADSGVKTFMN SFNELVFWGH AKDKRQAAMI ASRAGSDLDM
     EGYVYVNELV KLVEDGIVKE SIVDDAVRRI LKVKFELGLF DDPYKYCDPE NEKKNIGNVA
     HHEAVLDIAK KSIVLLKNEG NLLPLKKEGQ KIALIGPLAA DKNS
//
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