ID A0A286UD71_9AGAM Unreviewed; 1022 AA.
AC A0A286UD71;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=PNOK_0757200 {ECO:0000313|EMBL:PAV17507.1};
OS Pyrrhoderma noxium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Hymenochaetaceae; Pyrrhoderma.
OX NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV17507.1, ECO:0000313|Proteomes:UP000217199};
RN [1] {ECO:0000313|Proteomes:UP000217199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199};
RA Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M.,
RA Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N.,
RA Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F.,
RA Kikuchi T., Tsai I.J.;
RT "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its
RT Hymenochaetales Members.";
RL bioRxiv 0:0-0(2017).
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}.
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:PAV17507.1}.
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DR EMBL; NBII01000007; PAV17507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286UD71; -.
DR STRING; 2282107.A0A286UD71; -.
DR InParanoid; A0A286UD71; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000217199; Chromosome 7.
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:SF165; BETA-GALACTOSIDASE; 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, ECO:0000313|EMBL:PAV17507.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217199};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1022
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013561416"
FT DOMAIN 391..577
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1022 AA; 111717 MW; F5C1BBFDB3AC5526 CRC64;
MKLNQPVLGL LIVVLLFLHD SLTLGFSAGE DVFPKYQRQF SSGGVTDQVQ WDQYSLILKG
QRIFLHSGEF HTFRLPVPSL WLDILQKIKA AGLNGISVYL HWGAINPSRG VIDFDGIRSL
QTLFDLAKSV GLWVVLRPGP YMNAETTAGG IPHWVTAEVA GTLRTNATDY HETWEEYIDA
LIKFILPNQI NEGGPLIAVQ IDNEYSQGGF GHAEYFQELE GAYRAGDVVI PLTYNDPGQR
KNFVNGTGAV DIYGLDQYPQ GFDCSNPLRW SSVVGNNHDY HLDTNPSQPF YIPEFQGGAF
DPWGPTAPGY PNCQILTGPD FEDVFYKALW ADNVKLLNFY MLYGGTSWGS IPFPGVYTSY
DYGSSIQENR LLTPKYTELK QQGIFLRSSP DFYKTAWVGN SSSSAVNVSN PDIFAVFLSN
PDTSSGFYIT RHSDSTSTET TEFTLDVSTS LGSLTVPKTI PSITLSGRQS KLVVTDYTFG
VSSKLLYSTA TVFFAGQIGS RDVLFLSGDS DQQHEFAVFL NNGSSVVSDT RLQASQSASL
GGETTIAVLG NLTGLLTVFE SDSQLILFGD SDTAGTFFSP VIPASEKGDF SHYWQFGSNA
SVLVGGPYLV RNATISEDGS ALSLWGDLSE DVDLTVFAPD KVKAVEWNGR VVGSLESKSG
KLVGKLELEG KEGDVVLPAL SDWRFANSLP EIQDGFDDRS WTIANKTSTN SPFKPFYGDG
RVLYGCDYQF CENIVLWRGH FNGTGSEKSV NLSINGGEAF AASVWLNDVF LNTSFGNSTN
NRHILEETDD KFDFPEGSVR IGRDNVITVV QDNMGLNETQ SDPDTSKSPR GIRGFKLNDG
SFGEWKVQGK VGGYTKFLDR TRGIVNEGGL FGEREGWHLP GFDTSSWTKR NLSDGLPNGT
AGVGFFVTKF NLDVPKGRDV PLSFVFDGDQ TGVGAPYRAI LFVNGWMMGK RVGNLGPQTK
FPVHEGILDY HGENTVAVAL WSLLPDGSGV SVEPTLDLVL DGYIEGGVGG IEVNNPGYLD
RV
//