ID A0A0A0LUR1_CUCSA Unreviewed; 738 AA.
AC A0A0A0LUR1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=Csa_1G085360 {ECO:0000313|EMBL:KGN64739.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN64739.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN64739.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
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; CM002922; KGN64739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0LUR1; -.
DR STRING; 3659.A0A0A0LUR1; -.
DR EnsemblPlants; KGN64739; KGN64739; Csa_1G085360.
DR Gramene; KGN64739; KGN64739; Csa_1G085360.
DR OMA; CGNYNHG; -.
DR Proteomes; UP000029981; Chromosome 1.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
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; 2.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR041392; GHD.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
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:SF124; BETA-GALACTOSIDASE 2-RELATED; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 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; PS50228; SUEL_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..738
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001973149"
FT DOMAIN 652..738
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 738 AA; 80942 MW; C4B270994E0D47AE CRC64;
MKGLRFAVVF VLLLLGVLHS FSLAVNVTYD HRALVIDGKR KVLVSGSLHY PRSTPEMWPG
IIQKSKDGGL DVIETYVFWN LHEPVRNQYD FEGRKDLVKF IKLVGAAGLY VHVRIGPYVC
AEWNYGGFPV WLHFVPGVQF RTDNEPFKAE MKRFTAKIVD VLKQEKLYAS QGGPIILSQI
NTCNGFYCDQ FTPNSNNKPK MWTENWSGWF LSFGGALPYR PVEDLAFAVA RFYQTGGSLQ
NYYMYHGGTN FGRTSGGPFI ATSYDYDAPI DEYGLVRQPK WGHLRDVHKA IKMCEEALVS
TDPAVTSLGP NLEATVYKSG SQCSAFLANV DTQSDKTVTF NGNSYHLPAW SVSILPDCKN
VVLNTAKINS VTTRPSFSNQ PLKVDVSASE AFDSGWSWID EPIGISKNNS FANLGLSEQI
NTTADKSDYL WYSLSTDIKG DEPYLANGSN TVLHVDSLGH VLHVFINKKL AGSGKGSGGS
SKVSLDIPIT LVPGKNTIDL LSLTVGLQNY GAFFELRGAG VTGPVKLENQ KNNITVDLSS
GQWTYQIGLE GEDLGLPSGS TSQWLSQPNL PKNKPLTWYK GINLERVLIS CLYHVPQSWL
KPTGNTLVLF EEIGSDPTRL TFASKQLGSL CSHVSESHPP PVEMWSSDSK QQKTGPVLSL
ECPSPSQVIS SIKFASFGTP RGTCGSFSHG QCSTRNALSI VQKACIGSKS CSIDVSIKAF
GDPCRGKTKS LAVEAYCQ
//