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Database: UniProt/TrEMBL
Entry: D7UBN6_VITVI
LinkDB: D7UBN6_VITVI
Original site: D7UBN6_VITVI 
ID   D7UBN6_VITVI            Unreviewed;      1114 AA.
AC   D7UBN6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE   AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN   OrderedLocusNames=VIT_13s0067g03000 {ECO:0000313|EMBL:CBI40151.3};
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:CBI40151.3, 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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR   EMBL; FN596752; CBI40151.3; -; Genomic_DNA.
DR   RefSeq; XP_002266400.1; XM_002266364.3.
DR   RefSeq; XP_010645604.1; XM_010647302.2.
DR   AlphaFoldDB; D7UBN6; -.
DR   STRING; 29760.D7UBN6; -.
DR   PaxDb; 29760-VIT_13s0067g03000-t01; -.
DR   EnsemblPlants; Vitvi13g01417_t001; Vitvi13g01417_P001; Vitvi13g01417.
DR   GeneID; 100241220; -.
DR   Gramene; Vitvi13g01417_t001; Vitvi13g01417_P001; Vitvi13g01417.
DR   KEGG; vvi:100241220; -.
DR   eggNOG; KOG2024; Eukaryota.
DR   HOGENOM; CLU_002346_0_2_1; -.
DR   InParanoid; D7UBN6; -.
DR   OMA; EITDFCH; -.
DR   OrthoDB; 276651at2759; -.
DR   Proteomes; UP000009183; Chromosome 13, unordered.
DR   ExpressionAtlas; D7UBN6; baseline and differential.
DR   GO; GO:0009341; C:beta-galactosidase complex; 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:0005990; P:lactose catabolic process; IBA:GO_Central.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032312; LacZ_4.
DR   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   Pfam; PF16353; LacZ_4; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT   DOMAIN          811..1096
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   1114 AA;  126083 MW;  56C2A24C9551C71B CRC64;
     MASLVAQLAF PSDYNRRVWE DPSFIKWRKK DAHVSLHCHD TVEGSLRYWY ERNKVDFIAS
     SSAVWNDDAV VGALDCAAFW VKGLPFVKSL SGYWKFYLAP GPTSVPMNFY DSSFEDSTWE
     TLPVPSNWQM HGFDRPIYTN IVYPFPLDPP HVPTENPTGC YRTVFHIPHE WKGRRILLHF
     EAVDSAFFAW INGVPVGYSQ DSRLPAEFEI TDYCHPCGSN KKNVLAVQVF RWSDGSYLED
     QDQWWLSGIH RDVLLLAKPQ VYIEDYFFKS NLGENFSYAD IQVEVKIDNS LETSKDSILN
     KFSIEAELFD SAKWHDSDEY CDLHSSSVAH MELDPSSSTA IFGFLGYVLV GKLESPKLWS
     AEQPYLYTLV VILKDEFGKV VDCESCQVGI RQVSKAPKQL LVNGHPVILR GVNRHEHHPR
     LGKTNMESCM VKDLVLMKQN NINAVRNSHY PQHPRWYELC DLFGMYMIDE ANIETHGFYD
     SQHLKNPTLE SSWASSMMDR VISMVERDKN HACIISWSLG NESGYGPNHS ALAGWIRGRD
     SSRLLHYEGG GARTPSTDIV CPMYMRVWDI VKIAKDPTEM RPLILCEYSH SMGNSNGNIQ
     EYWEAIDNTF GLQGGFIWDW VDQGLLKVGA DGAKHWAYGG DFGDIPNDLN FCLNGITWPD
     RTLHPAVHEV KYVYQPIKIS LSESTLKITN THFYETTKAM EFSWTVCGDG CKLGSGTLSL
     PIIEPQSSYS IEFESGPWYS LWASSSAEEH FLTITAKLLQ PTRWVEAGHV ISSTQILLPA
     KREFVPHVIK NKDAPVPGEI LGNTIRFYQQ NVWEIQFNAQ TGTIESWKVG GVTVMNKGIF
     PCFWRAPTDN DNGGGAKSYV SKWKAAHLDN LSFITESCSV QNITDHPVKL AVVYLGIPKG
     EENSLSRSEN PKVLLKVDIT YTVYGSGDII MECNVHPCSD LPPLPRVGVE FQLEKTIDQI
     KWYGKGPFEC YPDRKAAAHV GVYEQNVGDM HVPYIVPVEC SGRADVRWVT FQNKDGFGIY
     ASMYGSSPPM QMNASYYSTA ELERATHKEK LIKGDDIEVH LDHKHMGLGG DDSWSPCVHE
     KYLIPAVPYS FSIRLSPITA AITGYDIYKS QLQN
//
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