ID A0A164XP75_DAUCS Unreviewed; 797 AA.
AC A0A164XP75;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=DCAR_016669 {ECO:0000313|EMBL:KZM93424.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM93424.1};
RN [1] {ECO:0000313|EMBL:KZM93424.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM93424.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZM93424.1}.
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DR EMBL; LNRQ01000005; KZM93424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164XP75; -.
DR EnsemblPlants; KZM93424; KZM93424; DCAR_016669.
DR Gramene; KZM93424; KZM93424; DCAR_016669.
DR OMA; ICTIPVW; -.
DR Proteomes; UP000077755; Chromosome 5.
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; 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:SF179; BETA-GALACTOSIDASE 6; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF02140; Gal_Lectin; 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:UP000077755};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..797
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007854437"
FT DOMAIN 692..778
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 797 AA; 88140 MW; C926897CFE2CCC85 CRC64;
MGRSVCWAAG LVMMLVVAAA ADGGDVEYDG RSLIVNGKRK ILFSGSIHYP RSTPDMWPSL
ISKAKQGGLQ VIQTYVFWNL HEPTPGQYDF SGRNDIVGFI KEIQAQGLYV SLRIGPFIEA
EWTYGGLPVW LHDVPGIIYR TDNEPFKNLM HNFTAKIVGM MKSEGLYASQ GGPIILSQIE
NEYKNVESAF HEGGPAYVRW AAEMAVGLRT GVPWMMCKQD DAPDPVINAC NGMKCGETFV
GPNSPNKPSL WTENWTSFLQ TYGEEAPIRS AEDIAYNVAL FIVTKNGSFI NYYMYHGGTN
FGRTGAAYII TSYYDQAPLD EYGLTRQPKY GHLKELHAAV DSCSETILSG TKNNLSLGQS
QQAYVYQGKS GECAAFLVNT DKRETVHVNT QFNTRSMIPS LRLNSAERWE MFSEPIPQYN
EAIIKANMLL EQTSTTKDVS DYLWYTFSLQ KNSSDSKSTL NVDTLGHAIL AYVNGDFVGS
AHGSRKTNTP SLQSQIQLNR GVNKIALLSV MVGLKDSGAF LEHVYTGIRS VTIQDKQTSN
YTHYPWGYQV GLLGEKLQVY TSTGSSKVEW NKYSSSKQLT WYKTVFDEPE GSEPVALNLG
SMGKGEAWVN GQSIGRYWVS FHTPAGKPSQ TSYHVPRSFL KPKGNLLVLF DEEFGNPLDI
SIDTVSVTKV CTHISESSDR IISSKGDKKK KQETSAKAHL RCPPKKFISK ILFASFGTPL
GDCENYSVGR CHASNSKAVV ERACVGKREC SVGLSSKKFK GDPCPGVPKH LIIQAQCHSH
PDLSLNLTAR EQSNLLS
//
