ID D7SP52_VITVI Unreviewed; 845 AA.
AC D7SP52;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 85.
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 OrderedLocusNames=VIT_04s0023g02690 {ECO:0000313|EMBL:CBI17431.3};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI17431.3, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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}.
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DR EMBL; FN594959; CBI17431.3; -; Genomic_DNA.
DR RefSeq; XP_010649088.1; XM_010650786.2.
DR AlphaFoldDB; D7SP52; -.
DR STRING; 29760.D7SP52; -.
DR PaxDb; 29760-VIT_04s0023g02690-t01; -.
DR EnsemblPlants; Vitvi04g01389_t001; Vitvi04g01389_P001; Vitvi04g01389.
DR GeneID; 100232848; -.
DR Gramene; Vitvi04g01389_t001; Vitvi04g01389_P001; Vitvi04g01389.
DR KEGG; vvi:100232848; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; D7SP52; -.
DR OMA; ETTGHAM; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000009183; Chromosome 4.
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; 2.
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: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; 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:UP000009183};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..845
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003105805"
FT DOMAIN 755..841
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 845 AA; 94119 MW; FBC7AC0D1782785B CRC64;
MEANSVSKLF LVLCMVLQLG SQLIQCSVTY DRKAIVINGQ RRILISGSIH YPRSTPDMWE
DIIQKAKDGG LDVVETYVFW NVHEPSPGSY NFEGRYDLVR FIRTVQKAGL YAHLRIGPYV
CAEWNFGGFP VWLKYVPGIS FRTDNEPFKR AMQGFTEKIV GLMKSERLFE SQGGPIILSQ
IENEYGVQSK LLGDAGHDYM TWAANMAVGL GTGVPWVMCK EEDAPDPVIN TCNGFYCDAF
SPNKPYKPTI WTEAWSGWFN EFGGPLHQRP VQDLAFAVAR FIQKGGSFVN YYMYHGGTNF
GRTAGGPFIT TSYDYDAPID EYGLVRQPKY GHLKELHRSI KLCERALVSA DPIVSSLGSF
QQAHVYSSDA GDCAAFLSNY DTKSSARVMF NNMHYNLPPW SISILPDCRN AVFNTAKVGV
QTAHMEMLPT NAEMLSWESY DEDISSLDDS STFTTLGLLE QINVTRDASD YLWYITRIDI
GSSESFLRGG ELPTLILQTT GHAVHVFING QLTGSAFGTR EYRRFTFTEK VNLHAGTNTI
ALLSVAVGLP NVGGHFETWN TGILGPVALH GLNQGKWDLS WQRWTYKVGL KGEAMNLVSP
NGISSVDWMQ GSLAAQRQQP LTWHKAFFNA PEGDEPLALD MEGMGKGQVW INGQSIGRYW
TAYANGNCQG CSYSGTYRPP KCQLGCGQPT QRWYHVPRSW LKPTQNLLVV FEELGGDPSR
ISLVRRSMTS VCADVFEYHP NIKNWHIESY GKTEELHKPK VHLRCGPGQS ISSIKFASYG
TPLGTCGSFE QGPCHAPDSY AIVEKRCIGR QRCAVTISNT NFAQDPCPNV LKRLSVEAVC
APITS
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