ID A0A2T4GXB4_FUSCU Unreviewed; 1020 AA.
AC A0A2T4GXB4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=FCULG_00005790 {ECO:0000313|EMBL:PTD08194.1}, HYE67_001637
GN {ECO:0000313|EMBL:QPC59406.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD08194.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD08194.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD08194.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QPC59406.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Class2-1B {ECO:0000313|EMBL:QPC59406.1};
RA Yuan Z.;
RT "The chromosome-scale genome resource for two endophytic Fusarium species:
RT F. culmorum and F. pseudograminearum.";
RL Submitted (NOV-2020) 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; PVEM01000006; PTD08194.1; -; Genomic_DNA.
DR EMBL; CP064747; QPC59406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4GXB4; -.
DR OMA; GGCPGDI; -.
DR Proteomes; UP000241587; Unassembled WGS sequence.
DR Proteomes; UP000663297; Chromosome 1.
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:UP000241587};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1020
FT /note="Probable beta-galactosidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033324559"
FT DOMAIN 399..577
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1020 AA; 113429 MW; 184CE181E6A8FADC CRC64;
MKLLSLSTVG LLALTGFSIA QENANVPIQD NGLTNIVQWD DHSYLINGER IFVFSGEFHY
WRLPVPELWR DLLEKIKAAG FNAFSIYNSW GYHEASPGAL DFKNGAHDFE SIMTLAKELG
LYLLIRPGPY VNAEANAGGF PLWVTTGEYG KLRNDDPRFT KAWSKYWTEI SKVIEPHLIT
NGGNVAMFQI ENELGGQWKN DDKRILNEPV ANYMQLLKDA ARDAGIDVPV FHNAPNTRTF
SWSNDFEANA TGNVDVTGVD SYPSCWSCNL DECTGTNGEY VPYNIQDYVT YFSKQSPAQP
HFLPEFQGGS YNPWGGPEGG CPGDIGPDFA NIFYRDLVAQ QATAISLYMM YGGTNWGWFA
CPVVATSYDY SSPISENREI WDKYYETKSL TLFTRVAHDL TKTNRVTNST SLSTNDDVLV
TELRHEDNGA AFYVSRHDHS PSGTKETFKI RVNTSEGKLT IPQNDHITIN GHQSKIIPTD
FHFGEKTLLY TTAEVLTYSV IDKKEVIVLW LPEGEHGEFT LKGHTELKHD KSLKGINVKA
GKKSITVNYT QKKGLFTLNM KDGSTIVLAD RQTAYKFWAP TLDNDPFAPV NKTVLVHGPY
LVRHATVKNG QLNIEGDLDK STDITVFASE SLKSISWNGE KVKVSSKEGH KYTAKLKGPS
KVKLPKLESW KYTDSLPEIK SDYKTSSSTW VVANKKNTTN AVLVPDLKNP VLYVDEYNVH
YGNHIYRATF STTDKAPTGV YLNLTGGLAF GYSVWLNSDY VGSYLGNATV GRSGQEFSFK
NATLSKKENV LVVLMDNSGH DLRDGALDPR GITNATLIGS AKGGYKFSEW KIAGHAGSVE
GEVIDPVRGP LNEGGLYAER IGAHLPGFSD KKWKSFSSKQ GTLVNPSAGV RAYRTTVDLD
IPDGLDVGIS FKLTAPSNTT FSPTKKGYSN RVRVLLFVNG YQYGRFNPYI GNQVSFPVPP
GVLNYSGENT IAVTVWSQSA EGGEVKVEWE VDYVHSSSFD VKFDSEYLRP EWTEDRLQYA
//
