ID A0A2H3TQG6_FUSOX Unreviewed; 1002 AA.
AC A0A2H3TQG6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN ORFNames=FRV6_14033 {ECO:0000313|EMBL:SCO89905.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO89905.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMJY01000008; SCO89905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3TQG6; -.
DR VEuPathDB; FungiDB:FOC1_g10001597; -.
DR VEuPathDB; FungiDB:FOC4_g10007788; -.
DR VEuPathDB; FungiDB:FOIG_15038; -.
DR VEuPathDB; FungiDB:FOMG_14182; -.
DR VEuPathDB; FungiDB:FOXG_11735; -.
DR VEuPathDB; FungiDB:FOZG_11860; -.
DR VEuPathDB; FungiDB:HZS61_016778; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000219369; 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; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF122; BETA-GALACTOSIDASE A-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.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1002
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013877581"
FT DOMAIN 389..565
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1002 AA; 110013 MW; 0777EF073DDD860B CRC64;
MKLSNFFFAA LAASSHAKNV LPRGTRPSNI LDSRALLQDI VTFDEHSLFI HGERVTIFSA
EIHPFRLPVA SLYPDLFQKV KAMGFNMVSF YVDWALLEGK PGEFRSEGAL DLQPFIDAAH
EAGIYLLARP GPYINAEVSG GGFPGWLQRV KGFLRTNATD YLAATDNYVA HVAKIIAKAQ
ITNGGPVILY QPENEYSAAQ GTPFPNHDYL KYVNDQVRKA GVVVPLINND AWQGGTGAPG
TGPGAVDIYG HDGYPVGFDC ANPYTWPKDG LPTTWHAEHE KISPNTPYSI IEFQGGGFDP
PGGGGFDNCY ELTNHEFARI FYKNNLAAGV TIFNIYMTWG GTNWGNLGHS DGYTSYDYGA
AIKEDRTITR EKYSEIKLQG QFLRVSPNYA IAEASNFTTT KYTDNNNVAV TALTTKKDDA
FYVVRHADYR TTDSASYKLK VKTSTGTLTI PQLGGSLSLH RRDSKIHVVD YPVGKFKLLY
STAEVFTWKV LGDKTVLVLY GGADEVHEVA VKGQEKVKVV EGDGVKIEKK NGAGVFQFKT
STKRRVVQAG SLYIYLLDRN AAYKYWVPTI PSKKSGEYGS SVMNPDAVII NGPYLVRSVA
VEGSKLSVQA DFNITTPVEI IGAPKGTSRL SINGKDTSFT KSKLGNWLVN PEIKLPTVKV
PDVKSLDWHY IDGLPEVKKD YDDSKWRTAD IKKTLNSKWP LNNSVSLYSG DYGFNAGALI
FRGHFTASGS ESKLKLWTFG GRAYGSSVWL DDKFVGSVTG GGNNNNDTST YKLPKTEKGK
KHVVTVIVDN MGLNGNWVPG VDETKQPRGI LDWHITSDSG KETKVSKWKL TGNLGGENYK
DKFRGPLNEG GFFFERQGYH LPSPPLTSFK SGSPFKGLSK PGVSFYTAKL PLNLPSSTHD
IPLSFTFKNN TSSTGAYRAI LYVNGFQYGK YVANVGPQTV FPVPEGILNY KGDNWIGIAL
WALEKSANVD GLSLTAGVAV QTGRKPVKVV EGPKYSRRQD AY
//
