ID F8QCG4_SERL3 Unreviewed; 1021 AA.
AC F8QCG4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=SERLA73DRAFT_171732 {ECO:0000313|EMBL:EGN93829.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
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; GL945490; EGN93829.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QCG4; -.
DR STRING; 936435.F8QCG4; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_0_1; -.
DR InParanoid; F8QCG4; -.
DR OMA; FYIARQT; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000008063; 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:EGN93829.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 371..555
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1021 AA; 111844 MW; B420A96BCC5DA461 CRC64;
MVRYQARSRV LHLRKREESS VGNLTSNGRT TEVEWDSYSL VIKGQRVFIH SGEFHTFRLP
VPGLWLDILQ KAKAAGFNAL SVYTHMALVN PSPGVIDFND YRALEPLYEA AKQTGIFIVL
RPGPYINAES TAGGIAHWIT SQVAGELRTN ATDWRASWQD YIQGIIDQTA PYQITQGGPV
IDNEYSQSGY GHAEYFAELE EVFHNSSIVV PLTANDPGEG RDWVNGTGAV DIYGLDSYPQ
GFDCSNPTVW SPVVTNYYSY HESVDPSEPW YFPEFQGGSF DAWGPTAPGY DQCRVLTGAD
FENVFNLNLW ASNAKLINYY MLYGGTSWGG LPFPGVYTSY DYGSAIAENR ELTTKYPELK
REGLFLRSSP EFYKTSWIGN SSTSAVIVSN SSAFVTLLRN PDTSTSFYIA RQNDSTSTGI
TTFKLNVTTS AGNLEIPQVV PEITLGGRQS KLIVTDYSFG SSNVLYSTAQ VLYAGQIGGR
DVLYLYGDST QEHEVSLVLT GTPRLQADTP HISSHLSTGQ GTIISFLSGI EGLVTVWDSS
EQLILYSDAD TAGTFWSPEI PSNATSGDAA TFSNYWQFGT NTSILVGGPY LVRNATITGS
TLNLRGDLND SVRLTVIAPE TVTSITWNGM DISADVAATS NLTTQGGFVA QIQPASGISS
IPVPTLSNWK YANSLPEIQS NFSDASWTLA NHTTTNIPFK PYYGDGRVLY GCDYEYCENI
VLWHGHFNAT ENTKSVNLSI NGGEAFAASV WVNDVFLNTS YGNSTNNANI VDETDEKFYF
PSGSLNYGQD NVITILQVST HIHLSSTDEL YVCVPKDNMG LDESGSEIDE EKSPRGVRGF
QLNTGDFGEW KVQGKIGGYT NYPDKVRGVL NEGGLYGERL GWHLPGFDTS IWESRDITEG
LPGSAAGVGF FVTTFDLQIP EYYDAPMSFT FDQSSQPYRV QLYVNGWMMG KRVANLGPQY
KFPVHQGILN YSGPNTVAIA LWAMEPTAIS PTVALTVDGV FEGGVGGIEV NNPAWSPEGR
Q
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