ID M7T455_EUTLA Unreviewed; 977 AA.
AC M7T455;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Probable beta-galactosidase B {ECO:0000256|ARBA:ARBA00040693};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase B {ECO:0000256|ARBA:ARBA00042633};
GN ORFNames=UCREL1_1554 {ECO:0000313|EMBL:EMR71392.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR71392.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans.
CC {ECO:0000256|ARBA:ARBA00002691}.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; KB705645; EMR71392.1; -; Genomic_DNA.
DR RefSeq; XP_007789502.1; XM_007791311.1.
DR AlphaFoldDB; M7T455; -.
DR STRING; 1287681.M7T455; -.
DR KEGG; ela:UCREL1_1554; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_1_1; -.
DR OMA; GGCPGDI; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000012174; 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; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF64; BETA-GALACTOSIDASE (EUROFUNG)-RELATED; 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.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 342..513
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 977 AA; 106487 MW; E762A3012B17499C CRC64;
MLHYWRYPVP ELWKDLLEKV KAAGFNAFSI YNHWGWHNPV PGVIDFESGA HDFTQLLTFA
KEIGLYVILR PGPYINAEAN AGGFPLWVTT GAYGELRDND PRYTEAWIPY MTEMAKQVKP
HLITNGGNVI LYQIENEYSE QWLDIEEKID NVPVQEYFEL LKNNAWDNGV DVPLMHNAPN
MNGYSWSKDF SDAKGNVDVV GLDSYPSCWS CNLSECTGTN GEYVPYKTQN YFDYFIVQSP
TQPHFMPEFQ GGSYNPWGGP QGGCPGDIGA DFANIFYRNL IYQRVSAVNL YMLFGGTSWG
WHAAPVVATS YDYSSPISES RSIGSKYYET KLLTQFTKIA KDLAMTDRLA ITTSELRNPE
TGAAFYVVMH ADTSSSTQET FKLSVNTSEG ALTIPQYGGN IAINGHQAKI LVTDFQFGSR
SLLYSTAEVL TYAVVDGKEV LVLWVPTGES AEFSISGLSN ATLTSCDKCA NVEIHPTDSS
VTVAFTQNAG KSIVTLEDGS KVVLLDRSAA YLFWAPSLSN DPMASPNSTI LVHGPYLVRS
ASIDDQSLSL TGDIANATTI SVFAPQAIST ITWNGRNLEI ASRENGIITA QIEGPKSFEL
SPLTGWEYTD GLPEIANDYD ATGDAWIVAN KTKTSNPTTP APNNPVLYVD DYGIHTGAHI
YRATFPSTNI DTSTSTNTTS PPPTGVYIHA IGGLAFGYSA WLNSHFIGSW LGLSYVDEQG
ITLSFGNATL HEGEENVLVV VMDNSGHDQR AEALNPRGIT NATLVGPSGD EKYAFSEWKI
AGAAGVGSGG VDPVRGILNE GGFYAERVGL HLPGYPGTEF QAVPVSSTSN SSDDDDNTSL
LQVEGAGVRV FRTIVPLAVP EGLDVSISFR LSAPSSPSSS SARRKTNQLR ALLFVNGYQY
GRFNPYIGNQ VDFPVPPGVL NYGGDNTVVV HVWSQSGEGA EVGVGWNVEF VHDTSYDMGF
DSAYLRPGWD EGRLVWA
//
