ID G2XBX8_VERDV Unreviewed; 995 AA.
AC G2XBX8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=VDAG_07660 {ECO:0000313|EMBL:EGY16496.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY16496.1};
RN [1] {ECO:0000313|EMBL:EGY16496.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY16496.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; DS572711; EGY16496.1; -; Genomic_DNA.
DR RefSeq; XP_009654860.1; XM_009656565.1.
DR AlphaFoldDB; G2XBX8; -.
DR EnsemblFungi; EGY16496; EGY16496; VDAG_07660.
DR GeneID; 20709123; -.
DR KEGG; vda:VDAG_07660; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_0_1; -.
DR InParanoid; G2XBX8; -.
DR OMA; GGCPGDI; -.
DR OrthoDB; 1032627at2759; -.
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..995
FT /note="Probable beta-galactosidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003439138"
FT DOMAIN 372..551
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 995 AA; 109551 MW; A851E5D3F94FD0DD CRC64;
MRLSTTAAAL AALGGLCAQA QNVTEWPLHD NGLNKVVQCY MINGERLFIF SGDPELWRDL
LEKMKAAGGY HEASPGVLDF TSGAHDFVSL MTIAKEVGIY LLIRPGPYVN AETNAGGFPL
WLTTGEYGSL RDDDPRYTKA WTPYWEEISK IIAPHLVTNG GNVAMFQIEN ELNGQWKDIG
RKILNPPIAN YMQLLQDSAR DSGIDVPVFH NAPNMRGYSW SKDFSNATGN VDTVGVDSYP
SCWSCNLSEC TNFNGEYVPY SVVNYYDYFQ VQSPSQPNFM PEFQGGSYNV WGGCPADTGA
DFANIFYRNL VYQHVTAISL YMMFGGTNHG WLSCPVVATS YDYSSPVSEN RKIGDKYYET
KLLPLFTRVA KDLYKTERVG NSTSYTNNPA IAASELRNID NDAGFYVVMH QTSSSGTRET
FKLDVKTSAG DLTIPQHSSI TINGHQAKIL VTDFSFGSKT LLYSTAEVLT YAVFNEKEVL
VLWLPEGESG EFVVNGVTDA QSGEQGLGKI DFYPGEDSIT VSYTQEKGIF NVELEDGSSV
VLLDRKAAYH FWAPQLDNNP FFVENKTVLV QGPYLVRHAS INETNRGLDL RGDLDGPTTV
TVFGPSSLCS ISWNGEKVAI ESRNGNEFTF SLDGPAKFEL PVLGSWKYDD SLPEIAPDYE
ASPSTWIVAD RNETSNTEIP DLSNPVLYVD EYKVHVGNHL FRATFPSTDE PPTGVFLNLT
GGLAFGYSAW LNGDYIGSYL GYSYLGAWAE ELSFDNATLA TEGENVLTVL MDNSGHDLRE
AALAPRGISN ATLIGPSSEA YRFSEWKIAG TAGGGQANID PVRGPLNEGG LYAERIGVHL
PGFSDESFTP YPLNATTLDV PGAGVRVYRT TVDLDVPAGL DVAISFRLTA PSDSTFQPTK
SGYSNRVRAL LFVNGYQFGR FNPHIGNQVH FPVPPGIWDY HGENAIAVTL WSQDANGSEI
KVELELDYVH TTSFDLGFDG EYLRPGWDEK RLEYV
//
