ID   A0A2G5DVF8_AQUCA        Unreviewed;       851 AA.
AC   A0A2G5DVF8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=AQUCO_01400261v1 {ECO:0000313|EMBL:PIA47491.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA47491.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA47491.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) 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}.
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; KZ305031; PIA47491.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5DVF8; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
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:SF67; BETA-GALACTOSIDASE 10; 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:UP000230069}.
FT   DOMAIN          771..851
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   851 AA;  95407 MW;  2ECDE35CC86A84A4 CRC64;
     MAKRNFSFAI LLFFFFFLFF FLFSFSLATN VSYDHRSLII DGQRKLLLSA SIHYPRSVPG
     MWPGLIKTAK EGGIDVIETY VFWNGHELSP GNYYFGGRYN LVKFVKIVQQ AGMHLILRIG
     PFVAAEWNFG GVPVWLHYVP GTVFRTDNEP FKNFTTYIVN MMKREKFFAS QGGPIILAQI
     ENEYGDIERI YGDGGKPYAM WAAKMAVAQD IGVPWIMCQQ YDAPDPVINT CNSFYCDQFT
     PNSPNKPKFW TENWPGWFKT FGSRDPHRPP EDVAFAVARF FQKGGSLNNY YMYHGGTNFG
     RTSGGPFITT SYDYDAPIDE YGIARLPKWG HLKQLHEAIK LCEHPMLHGE PTLLSLGSLQ
     EADVYTDSSG GCAAFISNMD EENEKTVYFQ NVSYHLPPWS VSILPDCKNV AFNTAKVGHQ
     TSIMEMVPEY LQASMTSPDK ESKAPKWGVY VEKAGIWGEA DFVKNGFVDH INTTKDTTDY
     LWYTTSFYVN ENEEILSNRN QATLVISSKG HALHAFVNQK LQGSASGNGL NSTFDFESPI
     LLKAGKNEIS LLSMTVGLQN AGPFYEWVGA GLTSVKVKGL KNGTVDLSSN AWTYKIGLEG
     EHLKIYQANG LNSVKWQSTS EPPKNQPLTW YKAVVDPPSG DEPVGLDMIE MGKGLAWLNG
     EEIGRYWPRR SSLHEECPSE CNYRGKFMPN KCSTGCGEPT QRWYHVPRSW FKPSGNILVI
     FEEKGGDPTK IKFSRRRTTS VCAHVSEDYP SFDLESWPKY TASTKKNIAT LHLKCPEGTL
     ISTIKFASFG TPTGKCGSYS KGDCHDPKSI AMVEKVCLNK KGCDIALSKD NFNMGLCPGL
     MKKLDVEAVC S
//