ID A0A1Z5SZS2_HORWE Unreviewed; 995 AA.
AC A0A1Z5SZS2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=BTJ68_09997 {ECO:0000313|EMBL:OTA27776.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA27776.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA27776.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA27776.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OTA27776.1}.
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DR EMBL; MUNK01000174; OTA27776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5SZS2; -.
DR STRING; 1157616.A0A1Z5SZS2; -.
DR VEuPathDB; FungiDB:BTJ68_09997; -.
DR InParanoid; A0A1Z5SZS2; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000194280; 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 Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..995
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012419127"
FT DOMAIN 375..552
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 995 AA; 109351 MW; 8DA0EA92FAB173EA CRC64;
MLFGRLCHAA LLSAAAVQSA TALAIGGKPN LMIRDSDSLQ DIVTWDEHSL FVHGERIIFY
SGEFHPYRLP VPSLWLDVFQ KIKALGYNGV SFYTDWALLE GKPGVFNASG VFDFQPFFDA
AQEAGIYLLA RPGPYINAEV SGGGFPGWLQ RIPGTLRTRD PSYLHATDNY ARNMNEIIAK
AQITNGGPVI LAQPENEYTG ATDDVPEFPD PVYFGYVEKQ MRDAGIVVPL ISNDASPQGY
FAPGSGSPAA VDIYGHDGYP LGFDCANPYT WPDQSLPTNF LTLHRQQSPS TPYSIIEFQG
GAFDPWGGNG FEQCVKLLGP EFERVFYKND FSFGLTIFNI YMTYGGTNWA TLGTQEATLP
KLEANFLQAS PAYWTAWAQN NTNANGSYTG NEDLAVTALL GEQTNFFVLR HAAFNSLETT
DYSITLPSKS QGNITIPQLG GSLSLHGRDS KWHVTDYDVG GVNLVYSTAE IFTWKQYGHK
RVLVVYGGPD EMHELAVEGG GHARTVEGDG VKYGKKNGAT VMQYSVSADR KVVELGCGLT
VYLLDRNSAY NYWVLDLPSD NVWGNYTHPS HAVSAPIVNG GYLLRTVEVK DGCVHLTGDI
NSTTTFEVIG GAPHHTREMT FNGEKVHFKQ DHWSGVVTAT VSYDEPSIDL PNLSTIGWKS
VDTLPELKSD YDDSLWTDAY LTYTNNTLRN LTTPRSLYAS DYGYNTGYLL FRGHFTAKGG
ESSLYLATQG GSAFGHSVWI NNTFVGSFDG ADLYSTWNAT YDLPTLSAGS PYVITVLIDN
MGLNEDWTVG TDDMKTPRGI LDYRLDGHRK DDITWKLTGN LHGEDYEDKT RGPLNEGGLW
VERNGYHLPG APTSDWTSSA LGPMEGLSEP GVKFYATTFD LDMPEGYDIP LSFSFSNATM
TSNGTAQAYR CQIYVNGYQF GKYVHNIGPQ DDFPVPEGIF NYHGSNYVGV SFWSLEEEGA
RVGNFSLVAG HPVQSGFGPV QLAPLTGWSK REGAY
//
