ID A0A0D2TWJ7_GOSRA Unreviewed; 844 AA.
AC A0A0D2TWJ7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=B456_008G036000 {ECO:0000313|EMBL:KJB47670.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB47670.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB47670.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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; CM001747; KJB47670.1; -; Genomic_DNA.
DR RefSeq; XP_012436366.1; XM_012580912.1.
DR AlphaFoldDB; A0A0D2TWJ7; -.
DR EnsemblPlants; KJB47670; KJB47670; B456_008G036000.
DR GeneID; 105762935; -.
DR Gramene; KJB47670; KJB47670; B456_008G036000.
DR KEGG; gra:105762935; -.
DR eggNOG; KOG0496; Eukaryota.
DR OMA; RKEPNIT; -.
DR OrthoDB; 1204541at2759; -.
DR Proteomes; UP000032304; Chromosome 8.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd22842; Gal_Rha_Lectin_BGal; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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 InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR PANTHER; PTHR23421:SF52; BETA-GALACTOSIDASE 14; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
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.
DR PROSITE; PS50228; SUEL_LECTIN; 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:UP000032304};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..844
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002265259"
FT DOMAIN 753..841
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 95309 MW; 3DE6B73F7B977E89 CRC64;
MVQVEPGRIL LITFLSTLLI TSSIAQKEDE EEVDPDSPES TTPKEVTYDS RSLLVNGKRM
LFFSGSIHYP RSPPDAWPDL IRKAKMGGLN MVETYVFWNV HEPVQGKYNF EGEYDLVKFI
KLIQQNKMFA MLRVGPFVQG EWNHGGLPYW LREVPNIIFR CDNEPFKMHM KKFVTLVIEK
MKQAKLFAPQ GGPIIVSQIE NEYNTIQLAF RERGDSYVQW AAKMALSLDT KVPWIMCKQK
DAPDPIINTC NGRHCGDTFT GPNGPNKPFL WTENWTAQFR VFGDPPSQRS AEDLAFSIIR
FCSKNGTLVN YYMYHGGTNF GRTSSSFTTT RYYDEAPLDE FGLIREPKWG HLKDAHRAVN
LCKRALFSGS PFVQKLGPDQ EARVWEQPGT SLCSAFLTNN NTKKPQALRF RGQDYQLPPR
SISILPDCKT EVFNSQMITT HHNSRNIVRS IAANKNFNWE MYREVVPDDP GNKLNEPREL
YELTKDTSDY AWYITKLDLG RRDLPMKNEI LPVLRVASLG HGLHCYVNGK YIGSAHGSKV
EKSFVFQKPV EFQAGSNQIA LLGFLVGLPD SGAYMEKRYA GPRSITILGL NTGTLDITLN
TWSHQVGLDG EKNQIYTQNG FPKVQWVKGG PSEGVTWYKG YFDAPEGDNP VAVKMTGMGK
GMVYINGRNI GRYWMSYLSP LKRPTQSEYH IPRSYLQPTM NLIVIVEDEK GDPKNIEIVL
VDRDTICGFI TENHLPSVRL FEGKGGKLVA LEKDLKPRVE LACPGQKQIV AVEFASFGDP
FGACGHYVEG NCTSPVAKQV VEKFCLGKPS CKIPLDTPDL HNKNEACPEM KKTLAIQAKC
AFKA
//
