ID A0A165HWQ4_9APHY Unreviewed; 1053 AA.
AC A0A165HWQ4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=LAESUDRAFT_746914 {ECO:0000313|EMBL:KZT12288.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT12288.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT12288.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT12288.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV427606; KZT12288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165HWQ4; -.
DR STRING; 1314785.A0A165HWQ4; -.
DR InParanoid; A0A165HWQ4; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:KZT12288.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 444..626
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1053 AA; 115222 MW; 00B0C28D4D721B1A CRC64;
MLVDRPWENV LLSYRQAGLL RHYKDSGPET VGCRRARMVS SRCSRWAFPA LLSLLLVLLT
WPITRTTSAL SFRKNVRKAL QDVVTASEPT RKSDNYTDIV QWDNYTIFLN DQRMFLHSGE
FHTFRLPVPD LWLDIFQKMV AAGLNGVSIY VHWTLTNPAP GVLDFNDWRA LQPVFDAAKQ
AGIFVTLRPG PYINAETNAG GIALWATSLV AGELRTNATD YMEAWMPYVK EVAASVVPNQ
VTGGGPILLL QIDNEYEQNA VTGEYFVELE NTYREAGVVV PLTYNDPGEG QNFINGTGAV
DIYGLDSYPQ GFDCSDPIVW SSVVANYHQY HEETDPGEPW YMPEFQGGSF DPWGGTGYNN
CEILTGVDFE DVFYKQNWAS NVKMISYYMV YGGTSWGGLP YPGVYTSYDY GSSIRENRVL
SDKYDELKRQ GLFLRSSPEF RKTDWIGDTD TGMPGVVVNG SEAYVTWLRN PDSGTGFYIV
RQSNSSSMAD ITFRISVPTS EGTLSIPRTI DSIAINGRQS KVLVVDYSYG ANSSVLYSTA
SVFFAGTIGS RDVLFLYGDT DQSNEIALTL KGSGTKASSS QVSISNAGTG GYSTITLLAG
IEGLIPLYES DSQLILYSDP VTAATYWAPV IPSTTATSFE NYWQFGSNST ILVGGPYLVR
NASLSSGHLA LRGDLNKSII LTVVAPEEVT SISWNGVEVD AVNIADGILS GNLTISSSLK
SITVPSLAGW RYADSLPEVL SNFSDADWII ANHTTTNITP GPLYGDGRVL FGCDYGFCEN
IVLWRGHFNG TGSETSANLT INGGDAFAGS VWINDRFINS TWDVSAEQTT ALYTFPEESV
RIEEDNVITV IQDGMGNDEN PDEKSPRGIP GFLLTGGSFT EWKVQGKMGG YTNYPDKVRG
VLNEGGLYGE REGWHLPGYD TSSWEERDLS DGLPSGGAGV GFFVTTFDLS IPEGTDVLIS
FQFDTMDQPY RATLFVNGWN YGKRVANIGP QSKFPVHQGL LDYSGTNTVA VALWALQDTA
VSPTLELVVD TVIEGGVGEI GVNNPGWSAR VIA
//
