GenomeNet

Database: UniProt
Entry: A0A0A0LUR1_CUCSA
LinkDB: A0A0A0LUR1_CUCSA
Original site: A0A0A0LUR1_CUCSA 
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
//
DBGET integrated database retrieval system