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Database: UniProt
Entry: A0A0A0KMB2_CUCSA
LinkDB: A0A0A0KMB2_CUCSA
Original site: A0A0A0KMB2_CUCSA 
ID   A0A0A0KMB2_CUCSA        Unreviewed;       750 AA.
AC   A0A0A0KMB2;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=Csa_6G504610 {ECO:0000313|EMBL:KGN48881.1};
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:KGN48881.1, ECO:0000313|Proteomes:UP000029981};
RN   [1] {ECO:0000313|EMBL:KGN48881.1, 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}.
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DR   EMBL; CM002927; KGN48881.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0KMB2; -.
DR   EnsemblPlants; KGN48881; KGN48881; Csa_6G504610.
DR   Gramene; KGN48881; KGN48881; Csa_6G504610.
DR   OMA; ETTGHAM; -.
DR   Proteomes; UP000029981; Chromosome 6.
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; 3.20.20.80; Glycosidases; 2.
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; 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:SF79; BETA-GALACTOSIDASE 3; 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; 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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..750
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001965262"
FT   DOMAIN          652..738
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   750 AA;  83271 MW;  E42FF92F26822373 CRC64;
     MATNSVSKLS MLVLGLFWLL GVQFVQCSVT YDRKAILING QRRVLFSGSI HYPRSTPEMW
     EGLIQKAKEG GLDVVETYVF WNVHEPSPGN YNFEGRYDLV RFIKTIQKAG LYANLRIGPY
     VCAEWNFGGF PVWLKYVPGI SFRTDNEPFK RAMQGFTEKI VGLMKSENLF ESQGGPIILS
     QINTCNGFYC DAFSPNRPYK PTMWTEAWSG WFNEFGGPIH QRPVQDLAFA VALFIQKGGS
     FINYYMYHGG TNFGRTAGGP FITTSYDYDA PIDEYGLIRQ PKYGHLKELH RAVKMCEKAL
     VSADPIVTSL GSSQQAYVYT SESGNCAAFL SNYDTDSAAR VMFNNMHYNL PPWSISILPD
     CRNVVFNTAK VGVQTSQLEM LPTNSPMLLW ESYNEDVSAE DDSTTMTASG LLEQINVTKD
     TSDYLWYITS VDIGSTESFL HGGELPTLIV QSTGHAVHIF INGRLSGSAF GSRENRRFTY
     TGKVNFRAGR NTIALLSVAV GLPNVGGHFE TWNTGILGPV ALHGLDQGKL DLSWAKWTYK
     VGLKGEAMNL VSPNGISSVE WMEGSLAAQA PQPLTWHKCQ QGCGQPTQRW YHVPRAWLKP
     KDNLLVVFEE LGGNPTSISL VKRSVTGVCA DVSEYHPTLK NWHIESYGKS EDLHRPKVHL
     KCSAGYSITS IKFASFGTPL GTCGSYQQGT CHAPMSYDIL EKRCIGKQRC AVTISNTNFG
     QDPCPNVLKR LSVEVVCAPA TTAAEPNWRG
//
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