ID J5KA04_BEAB2 Unreviewed; 631 AA.
AC J5KA04;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN ORFNames=BBA_00616 {ECO:0000313|EMBL:EJP70986.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP70986.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP70986.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP70986.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
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|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; JH725150; EJP70986.1; -; Genomic_DNA.
DR RefSeq; XP_008593935.1; XM_008595713.1.
DR AlphaFoldDB; J5KA04; -.
DR STRING; 655819.J5KA04; -.
DR GeneID; 19883628; -.
DR HOGENOM; CLU_007853_7_2_1; -.
DR InParanoid; J5KA04; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000002762; 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; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
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; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..631
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003784017"
FT DOMAIN 35..358
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 402..513
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 534..596
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 183
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 260
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 631 AA; 68925 MW; AEC31FC769DA5FE4 CRC64;
MKLLLGALAA LSALSAAVAA GGASTPGNFS YNRHQFLLNG QPYQIIGGQM DPQRIPPEYW
THRLKMARAM GLNTIFSYLY WNLHEPSPGE WDFQGRNNVA EFFRLAQEEG LKVVLRPGPY
ICGERDWGGF PAWLSQVPGM AVRQNNGPFL DAAKSYINRV GKELGSLQIT QGGPILMTQL
ENEYGSFGTD KEYLAALAAM LHDNFDVFLY TNDGGGKSYL EGGQFHGVLA VIDGDSKTGF
EARDKYVTDP TSLGPQLNGE YYITWIDQWG SDYSHQQSSG SQTKIDKAVG DLDWTLAGNY
SFSIYMFHGG TNFGFENGGI RDDGPLAAVT TSYDYGAPLD ESGRPTDVYY SLREMISKHV
PAGSIPNVPT TPKRASVPAF KLQSGAALFD LKGAPTKKAN DPISMDALKQ AYGYVLYEYA
VTKELKGNVT IGDGARDRAM IYVNGVRVGV VDTIYKTPAT VTVALNKGDT LHILVENLGR
VDVRQRLKEQ VKGIVGNVTV GGQKLSNWAM YSIPLDKLPS GLDKKHTIKK NDTPVFYTGT
FGMPKGASAD PSGDTFITVP SAVKGVLWVN GVNMGRYWTV GPQQSLYVPG SILKEKNDVV
LLELEPQPEM KLSAEGLSER KWFNNPDPDA P
//