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Database: UniProt
Entry: S8E0R6_9LAMI
LinkDB: S8E0R6_9LAMI
Original site: S8E0R6_9LAMI 
ID   S8E0R6_9LAMI            Unreviewed;       634 AA.
AC   S8E0R6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE   Flags: Fragment;
GN   ORFNames=M569_05474 {ECO:0000313|EMBL:EPS69288.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS69288.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS69288.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
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:EPS69288.1}.
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DR   EMBL; AUSU01002191; EPS69288.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8E0R6; -.
DR   OrthoDB; 5489808at2759; -.
DR   Proteomes; UP000015453; 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; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
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; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015453}.
FT   DOMAIN          10..335
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          378..504
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          549..608
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        158
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        241
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EPS69288.1"
FT   NON_TER         634
FT                   /evidence="ECO:0000313|EMBL:EPS69288.1"
SQ   SEQUENCE   634 AA;  72033 MW;  1C49D362B9289EAE CRC64;
     RKFEIKDDMF WKDNKPFRII GGDLHYFRVH PEYWEDRLLR AKALGLNTIQ TYVPWNLHEP
     RKGELVFHGF ADIVSFLKLC EKLDLLVMLR AGPYICGEWD LGGFPSWLLT KDPPIRLRSS
     DPAFIELVNS WWSILLPKIH PLVYRNGGSV VMIQIENEFG SFGDDKAYLH NLVVLARSHL
     GSDVVLYTTD GGTRETLEKG TIMGDDVFSA VDFSTGDDPW PIFQLQKKFN PPGKSPPLSA
     EFYTGWLTHW NEEIASTDAE FTATYLEKIL SMNGSVVLYM VHGGTNFGFY SGANTGVDES
     DYKPDLTSYD YDAPIREYGD VKNAKYEALR KVIAKYGEVV SVPPDNEKTA YGRIKLEKQS
     SLFDMISYRS HVLHSKNPIS MEAAFQQMFG FVLYSSEYVP RTNGSSTTLI ISIGFILQVH
     DRAQVFISCP EKRPTYIGLI TRSSNRRAVD LPYLKCGQGK NKLLILVENM GHLNYGPYIF
     DRKGILSSVY LDGREHYEWE MFPISLQNLN EDINPDIAAK IHRKGLAYTN VGYLTGMYSS
     SADDLYQEPA FYVGHFHVER VGDTFISFRD WSKGIAFVNN NNIGRFWPSV GPQCSLYVPA
     PFLREGTNTL VILELESPSS ELYVSSVDHP DFTC
//
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