ID A0A0C9ZF51_9AGAM Unreviewed; 1045 AA.
AC A0A0C9ZF51;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=PISMIDRAFT_645777 {ECO:0000313|EMBL:KIK24544.1};
OS Pisolithus microcarpus 441.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK24544.1, ECO:0000313|Proteomes:UP000054018};
RN [1] {ECO:0000313|EMBL:KIK24544.1, ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|EMBL:KIK24544.1,
RC ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; KN833715; KIK24544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9ZF51; -.
DR STRING; 765257.A0A0C9ZF51; -.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000054018; 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; 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:KIK24544.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054018};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1045
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002218014"
FT DOMAIN 421..601
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1045 AA; 114774 MW; 5E22782B186A8C9B CRC64;
MRTPESRTRR RPLVLLLALV AVLYVLASLP GPLGLLGPWS SILATVASIL HAFPSRPPLV
RDAQSTTTTN LTGNGRTTDV LWDKYSLVIK GQRVFIHSGE FHTFRLPVPD LWLDILQKAK
AAGFNAVSIY THMGLINPSP GVIDFSDYRA LKPLYEAAKQ VGVWIVLRPG PYINAETTAG
GIAHWVTSQV AGELRTNATD WNAAWQLYIQ GVIRETAPYQ IDRGGPVIDN EYSQSPATHA
AYFEEVEDVY HNSDIVVPLT TNDAAEGQNW INGTGSVDIY GLDSYPQGFD CSNPTFWSPV
VTNYYSYHES VNPGQPWYFP EFQGGSFDAW GPTAPGYERC RGLTGPDFES VFYLNLWASN
AKLINYYMLY GGTSWGALPF PGVYTSYDYG GAIAEDRQLT TKYHELKRQG LFLRSSPEFY
KTDYIGHTTT SALIATSSFV HVTTLRNPDT GASFHIVRHN DSTSTSTVNF KMNITTESKT
IQIPRVAPAI TLSGRQSKVI VADYSFGLSK VRYATAQVLY AGRIGSRDVL YLYGDPLQEH
EVALSLNGTP RIRAQSSTCQ WHTMNGVTTV SLLAGIEGLV TLWDSDQQLI LYSDAATAGT
FWSPEIPSDD GSDFASYWQF GTNTSILVGG PYLVRNATMA GSTLELRGDL NEGVRLTVIA
PDNVRMITWN GIPVSPDVNA ASTITSVGGF SADLSPSLSG LGLGLPKLSN WKYANSLPEI
QGDFSDANWT IANHTTTNIP FKPHYGDGRI LYGCDYEFCE NIVLWHGHFN ATEETKSVNL
SINGGEAFAA SVWVNDVFLK TSYGNSTNNK NIVQETDEVF HFPPGSLKCG EDNVITVVQV
FKDNMGLDQN GDDHVDDEKS PRGIRGFALN TGNFSEWRVQ GKLGGYTNFP DKVRGVLNEG
GLYGERQGWH LPGYNTSAWT ARELAEGLPS SSAGVGFFVT TFRLSIPEEF DAPISFTFDQ
STQPYRALLF VNGWMMGKRV ANLGPQYDFP VHQGILDYHG ENTVAVALWA MEPTPITPTL
KLTAKGVYEG GVGKIHVNNP GWSAR
//
