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Database: UniProt
Entry: J5KA04_BEAB2
LinkDB: J5KA04_BEAB2
Original site: J5KA04_BEAB2 
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
//
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