ID A0A0N0NI10_9EURO Unreviewed; 792 AA.
AC A0A0N0NI10;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=AB675_9976 {ECO:0000313|EMBL:KPI35301.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI35301.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI35301.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI35301.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) 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:KPI35301.1}.
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DR EMBL; LFJN01000041; KPI35301.1; -; Genomic_DNA.
DR RefSeq; XP_017995264.1; XM_018150555.1.
DR AlphaFoldDB; A0A0N0NI10; -.
DR SMR; A0A0N0NI10; -.
DR STRING; 1664694.A0A0N0NI10; -.
DR GeneID; 28742435; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000038010; 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; 1.
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; 1.
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; 1.
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:UP000038010};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..792
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005856797"
FT DOMAIN 398..579
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 792 AA; 86927 MW; 3CC2F7F8E6788AE8 CRC64;
MHVRSVLVAA AALISSAAAV AVPIHSQTPA GYLITRESDG LQDIVTWDEK SIFVRGERVV
IYSGEFHPFR LPVPDLWLDI FQKIKALGYN GVSFYINWAL LEGQQGTYRA SGIFALEPFF
EAASEAGIYL LARPGPYINA EVSGGGFPGW LDRVDAPYQF RTNNTNYINA TTLYAQSVGE
TIAKGQITNG GPIILAQPEN EYSAYTSNAI FPNDVYFGEV IDQLRNAGIV IPLISNDASP
KGLFAPGNPN YTVHVDIYGY DGYPQGFDCQ QPYYWKPGNL PTDWTMLHRN QSPSTPNSIV
EFQGGSFDPW GGYGFDNCAA LTNAQFERVF YKNNWSFQVT FFNIYMTYGG SNWGNLGHPQ
GYSSYDYGAV IREDRAVTRT KYSEAKLLAN FIKVTPGFAT AEVMLYTNTS YVSTPDLTVT
ALIGNDSNFG LYIVRHSQYQ SNDTTSYTLT LPASSGNVTI PQLSSISDHL ILDGRDSKVH
VVGYPVGQML LEYSTAEVFT WERFDNGTVL VLYGDADEVH EFALSSGNCS LESGKSSLVA
INSTAGQQIV QWSVTPEEKI VKCGSLTVYL LWRNEAYNWW TLELPADAPL SNFTSSNKTS
VIVKGGNLMR TAQIINGDLY LTGDINETTT ISIQGSPPYN DLYFNGMNMG ASPATIEYTA
PTLNLPDLNQ SAWQSLDSLP ELSSSYDDTK WPVADDSTTV SQFQPNTSEV LFAGQYGFHC
GSLIYRGHFT APSSGSELNL SLLTQGGQAY GYSLWLNSTN IYQFPGISTN DSNLHSMQLT
NLTAGAPYVL TA
//
