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Database: UniProt
Entry: B1KHD4_SHEWM
LinkDB: B1KHD4_SHEWM
Original site: B1KHD4_SHEWM 
ID   B1KHD4_SHEWM            Unreviewed;       862 AA.
AC   B1KHD4;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE   Flags: Precursor;
GN   OrderedLocusNames=Swoo_1149 {ECO:0000313|EMBL:ACA85442.1};
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA85442.1, ECO:0000313|Proteomes:UP000002168};
RN   [1] {ECO:0000313|EMBL:ACA85442.1, ECO:0000313|Proteomes:UP000002168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) 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};
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DR   EMBL; CP000961; ACA85442.1; -; Genomic_DNA.
DR   RefSeq; WP_012323788.1; NC_010506.1.
DR   AlphaFoldDB; B1KHD4; -.
DR   STRING; 392500.Swoo_1149; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; swd:Swoo_1149; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_9_1_6; -.
DR   Proteomes; UP000002168; 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; 2.60.120.430; Galactose-binding lectin; 1.
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   InterPro; IPR041443; Exop_C.
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   PANTHER; PTHR30620:SF77; BETA-GLUCOSIDASE BOGH3B-LIKE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF18559; Exop_C; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 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   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACA85442.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002168}.
FT   DOMAIN          81..406
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          447..663
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
FT   DOMAIN          695..849
FT                   /note="ExoP galactose-binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF18559"
SQ   SEQUENCE   862 AA;  93562 MW;  85291271FCE3E52B CRC64;
     MSVLAYKRSL LSITILAITM TSGCSKEVAP QKEDLEPKEG LQSYAFGGKA VDINIWPALE
     LPHRNSSEVE GKVAEILAGM TLEQKVAQMI QPEIRDISVE DMRQYGFGSY LNGGGAYPNN
     DKHALPSDWI ALAENMYQAS VDASLDGSSI PTMWGTDAVH GHNNVIGATL FPHNIGLGAA
     NNPELIREVA AITAKEVMVT GIDWVFAPTV AVVRDDRWGR TYEGYSEDPE IVLAYSAAIV
     EGLQGEASGD EFLSSEHVIS TVKHFLGDGG TEKGVDQGDN LIDEQGLFDL HGQGYVGGLV
     AGSQSVMASF NSWHGVKNHG NEYLLTDVLK TRMGFDGFVV GDWNGHGQVL GCTNETCPQA
     VNAGLDMFMV PTDAWKPLYE NTIAEVRSGQ ISQARIDDAV SRILRVKVRA GLFNKPSPAN
     RPLSGKLELI GHESHRQVAK QAVRESLVLL KNGHNTLPLS PKMRVLVAGD GANNIGKQSG
     GWSITWQGTD NQNSDFPGAS SIYDGIKETV LKAGGTATLD IAGQYSEENR PDVAIVVFGE
     EPYAEGNGDI DNLEYQRGDK RDLALLKRLK SEGIPVVSIF ITGRPLWVNP ELNASDSFVV
     AWLPGSEGDA VADVLFSSSD GQVVNDMTGK LSFSWPSTPM QAVVNRFDKD YQPLFKYGHG
     LSYADKGDSA LVSEIKPVDS DILRPLVILK NAVKAPWRLS IGTSADQDLI NTSLQTSGPV
     VMRTIDRVVQ EDARKFNLDG KEQGVIRFGA NFTRDLRAYE QGNTAVSFDI KLDEFTPQST
     QLSMVCDKAC GVPVALEEKF KQIAGTGWQT ISVDLACFEL SSDQLSKVQS PFLFSSKAKI
     TMSLSNIYWL PDYQGQPDVS CH
//
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