ID M7TS86_BOTF1 Unreviewed; 1010 AA.
AC M7TS86;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN ORFNames=BcDW1_4870 {ECO:0000313|EMBL:EMR86471.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR86471.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; KB707857; EMR86471.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TS86; -.
DR STRING; 1290391.M7TS86; -.
DR HOGENOM; CLU_005732_2_0_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR018954; Betagal_dom2.
DR InterPro; IPR037110; Betagal_dom2_sf.
DR InterPro; IPR025972; BetaGal_dom3.
DR InterPro; IPR036833; BetaGal_dom3_sf.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1010
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004085908"
FT DOMAIN 395..580
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1010 AA; 111714 MW; 4B3BA514306984FC CRC64;
MLIYFNLLLI SAWWIQGLFA LKVGSIQNAR IKVHKREVLQ DLVSWDEHSI IVRGERIMIY
SGEVHPFRIP SPGLWLDIFQ KIKAMGFTGV SFYTYWGLNE GNPGQVITDG VFSLDEFFDA
ATQAGIYLIA RPGPYINAET AAGGIPGWVL RIKGVIRSTD QDYLDSTQNY ASTIGKIIAK
AQITNGGPVI MVQPENEYAS WPGVTNFPSQ MNKDYMAFVE QQLLDAGVVV PFVVNDNLNI
GNFAPGSGLG EVDLYGIDAY PMRYDCGDPY IWPTYRFPKT WEVSHANYSP STPFTIGEFQ
GGGGDGWGGV GEDRCAILTN NDAIKVQFKN TYSFRVAIFN VYMIYGGTNW GNLGYHGGYT
SYDYGASITE DRQVWREKYS EMKLEANFLK ASAAYLTATA GHGENGTYGV PAEIAVTPLF
GAINKGTNGT RTNFYVVRHA DFTSLARTSY KFTINTSHGN ITIPQLGGSL VMNGRDSKIH
VTDYDIGGIN MIYSSAEVFS WAKNHNNERV LILYGGDRDN NEAAFPVSLG LPNVIEGHGV
DIRRIGEAWV LQWTVNQERR IVQIGKLRVY LLWQNEAYNY WSLELEAPAP IGNHTSPSKP
SIIVNGGYLL RTASIEGKQL KLTGDINATT NFEVISTPTE VTSLLLNGKL LHTEKSRNGN
LQAHISYSPP SIDLPNFTTQ QWHYIDSLPE LHPHYDDSLW TPLDHITTNN TLNLTTPTSM
YASDYGYHTG SLIYRGHFLS TGNETTFFAN TTGGAGFGHS IWLNSTFLGS WVGSGGNQTY
AQTFSLPSLK SGSPYVFTVL IDHMGQDEEA PGTDAIKFPR GFLDYSLSSH PQADVIWKMT
GNLGGEQFID RKRGPRNEGA MFAERQGYHL PNPPSDAWEI RNPVSDGIDN AGVGFFTTRF
NLSIPEGWDV PLGFVFNGTG TAGNYRTQLF VNGWQFGKYV NNLGPQTRFP IPEGILNHQG
TNTVALTLWS LDSEGANIGG FELAPNATIW SGYRKPTLVE GSGWSRREGY
//
