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Database: UniProt
Entry: A0A0B0PK51_GOSAR
LinkDB: A0A0B0PK51_GOSAR
Original site: A0A0B0PK51_GOSAR 
ID   A0A0B0PK51_GOSAR        Unreviewed;       741 AA.
AC   A0A0B0PK51;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN   ORFNames=F383_07738 {ECO:0000313|EMBL:KHG23756.1};
OS   Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG23756.1, ECO:0000313|Proteomes:UP000032142};
RN   [1] {ECO:0000313|Proteomes:UP000032142}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA   Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA   Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA   Wilkins T.A.;
RL   Submitted (SEP-2014) 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         ECO:0000256|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; KN426197; KHG23756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B0PK51; -.
DR   Proteomes; UP000032142; 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; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR041392; GHD.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF51; BETA-GALACTOSIDASE 5; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 2.
DR   Pfam; PF17834; GHD; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032142};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..741
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002077561"
FT   DOMAIN          35..339
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          362..418
FT                   /note="Beta-galactosidase beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF17834"
FT   DOMAIN          471..538
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   DOMAIN          633..718
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
SQ   SEQUENCE   741 AA;  82977 MW;  85E70BBDC1D886AB CRC64;
     METSSVSKLL IFFFSAFLAS SKLIQCSITY DKKAILINGQ RRILISGSIH YPRSTPEMWE
     DLIKKAKDGG LDVIDTYVFW NGHEPSPGNY NFEGRYDLVR FIKTVQKLGL YVHLRIGPYI
     CAEWNFGGFP VWLKYVPGIS FRTDNEPFKR AMQGFTQKIV QMMKNEKLFA SQGGPIILSQ
     IENEYGPESR ALGAAGHAYI NWAAKMAVEL NTGVPWVMCK EDDAPDPVIN ACNGFYCDGF
     SPNKPYKPTM WTEAWSGWFT EFGGPIHQRP VQDLAFGVAR FIQKGGSYVN YYMYHGGTNF
     GRTAGGPFIT TSYDYDAPID EYGLIRQPKY DHLKELHRAI KLCEHALVSS DPTVTSLGTY
     HQAHVFSSRQ GGCAAFLSNF HMKSAARVTF NNRHYDLPPW SISILPDCKN VAFNTALVGV
     KTSRIQMLPT NTKMFPWEAY GEDISSLGAS SRITAPGLLE QMNVTRDNSD YLWYTTSVDI
     SPSESFLRGG QKPTLNVDSA GHALHVFVNG QFSGSAYGTR ENRRFTYTGP VNLHAGTNHI
     ALLSVAVGLP NDGLHFETWK TGIQSVLLHG LNQGKKDLTW QKWSYQAHIT TLKQVGLRGE
     AMNLVSPHGA SSVEWIRGER IQGSLAARSR QSMTWYKTYF NAPGGNEPLA LDMRSMGKGQ
     VWINGQSLGR YWMAYAKGNC GTCSYLGTFR TTKCQSGCDQ PTQRWYHVPR SWLKPTKNLL
     VVFEELGGDV SKISLVRRSV L
//
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