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Database: UniProt
Entry: A1SR95_PSYIN
LinkDB: A1SR95_PSYIN
Original site: A1SR95_PSYIN 
ID   A1SR95_PSYIN            Unreviewed;       753 AA.
AC   A1SR95;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   OrderedLocusNames=Ping_0139 {ECO:0000313|EMBL:ABM02010.1};
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM02010.1, ECO:0000313|Proteomes:UP000000639};
RN   [1] {ECO:0000313|EMBL:ABM02010.1, ECO:0000313|Proteomes:UP000000639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37 {ECO:0000313|EMBL:ABM02010.1,
RC   ECO:0000313|Proteomes:UP000000639};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) 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; CP000510; ABM02010.1; -; Genomic_DNA.
DR   RefSeq; WP_011768569.1; NC_008709.1.
DR   AlphaFoldDB; A1SR95; -.
DR   STRING; 357804.Ping_0139; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; pin:Ping_0139; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_8_2_6; -.
DR   Proteomes; UP000000639; 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   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:SF120; BETA-GLUCOSIDASE C; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 2.
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:ABM02010.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000639};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..753
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002637368"
FT   DOMAIN          162..350
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          396..511
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          549..752
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
SQ   SEQUENCE   753 AA;  81137 MW;  087B2D6DF6D5159F CRC64;
     MKNKMNKVFS VTPIALAVFL AGCNNDVIET TQVVKAEFAQ TKLDARGVDL ISTDGYQFKD
     LNKNGILNVY EDWRKTVDER VGDLVSQMTL EEKVGMMLID TMNAAAYGSV NGTHVDYIEQ
     QKMTRFIFRN AILPQNEVDA LPIGERAPGG DIVTGRASAS ISPSEAAQYM NIVQELSEST
     RLGIPALFKS NARNHNDPNA RAGINVSAGA FSEWPKEAGL AATRDMELIG EFAQIMRTEW
     NAIGLRGMYG YMADLSTEPR WYRVHETFTE DSDLASEIMT VLVSNLQGKE VTPSSVVLTM
     KHFPGGGPQF LGLDPHYMAG QHQSYPTGNF DYHVKPFKAA IDAGVAALMP YYGIVGGGEW
     SLSNPDETNL DVGGIQLAEV VSDRVQDTVR VPYNGYSTTE GTPAGNVGIA FSKGILSDLL
     RRDLGFSGVI NSDTGIIGET NNGLSDTDTI QNNRAWGLQD KDKSEQLVVA IEAGTDVFSG
     FHSNSEVRTL VEQGLVSEAR IDESVKRLLK VQFELGLFEN PYVDPVRANA IVGNASFQEK
     ALLAQRKAVV LLDNKVAEGA VEAILPLPAA ANLYTMGMDS GVVEGYGYTV TNGDLEGERP
     SAAESDYALI RVRVTNKDTG LLVFGGADFK EVDVLDFTGM AAAGTWDITP SLTDIQAVMA
     EVGAENTVLS VYFRQPFVMD EASGLKDAGA ILATFGSKDN ALMDVVTGGF NPSGKLPFAL
     ANSSQAIIDQ ASDAPGYAEA DTLYPFGFGL SYE
//
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