ID   BGAL2_ORYSJ             Reviewed;         827 AA.
AC   Q8W0A1; B7EU06;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 122.
DE   RecName: Full=Beta-galactosidase 2;
DE            Short=Lactase 2;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os01g0580200, LOC_Os01g39830; ORFNames=P0672C09.21;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; AP003546; BAB84455.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF05319.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS72858.1; -; Genomic_DNA.
DR   EMBL; AK103045; BAG95853.1; -; mRNA.
DR   RefSeq; XP_015621619.1; XM_015766133.1.
DR   AlphaFoldDB; Q8W0A1; -.
DR   SMR; Q8W0A1; -.
DR   STRING; 39947.Q8W0A1; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; 39947-Q8W0A1; -.
DR   EnsemblPlants; Os01t0580200-01; Os01t0580200-01; Os01g0580200.
DR   GeneID; 4324191; -.
DR   Gramene; Os01t0580200-01; Os01t0580200-01; Os01g0580200.
DR   KEGG; osa:4324191; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   InParanoid; Q8W0A1; -.
DR   OMA; SYEMQAS; -.
DR   OrthoDB; 5489808at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
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:SF153; BETA-GALACTOSIDASE 2; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 2.
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.
DR   Genevisible; Q8W0A1; OS.
PE   2: Evidence at transcript level;
KW   Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..827
FT                   /note="Beta-galactosidase 2"
FT                   /id="PRO_0000294153"
FT   DOMAIN          741..827
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   ACT_SITE        182
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        251
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   827 AA;  91549 MW;  100D0225FF558261 CRC64;
     MAASAVAVAF VVAVAAVLAA AASAAVTYDR KAVVVNGQRR ILISGSIHYP RSTPEMWPDL
     IEKAKDGGLD VVQTYVFWNG HEPSPGQYYF EGRYDLVHFI KLVKQAGLYV NLRIGPYVCA
     EWNFGGFPVW LKYVPGISFR TDNEPFKAEM QKFTTKIVEM MKSEGLFEWQ GGPIILSQIE
     NEFGPLEWDQ GEPAKAYASW AANMAVALNT SVPWIMCKED DAPDPIINTC NGFYCDWFSP
     NKPHKPTMWT EAWTAWYTGF GIPVPHRPVE DLAYGVAKFI QKGGSFVNYY MYHGGTNFGR
     TAGGPFIATS YDYDAPIDEY GLLREPKWGH LKQLHKAIKL CEPALVAGDP IVTSLGNAQK
     SSVFRSSTGA CAAFLENKDK VSYARVAFNG MHYDLPPWSI SILPDCKTTV FNTARVGSQI
     SQMKMEWAGG FAWQSYNEEI NSFGEDPLTT VGLLEQINVT RDNTDYLWYT TYVDVAQDEQ
     FLSNGENLKL TVMSAGHALH IFINGQLKGT VYGSVDDPKL TYTGNVKLWA GSNTISCLSI
     AVGLPNVGEH FETWNAGILG PVTLDGLNEG RRDLTWQKWT YQVGLKGESM SLHSLSGSST
     VEWGEPVQKQ PLTWYKAFFN APDGDEPLAL DMSSMGKGQI WINGQGIGRY WPGYKASGNC
     GTCDYRGEYD ETKCQTNCGD SSQRWYHVPR SWLSPTGNLL VIFEEWGGDP TGISMVKRSI
     GSVCADVSEW QPSMKNWHTK DYEKAKVHLQ CDNGQKITEI KFASFGTPQG SCGSYTEGGC
     HAHKSYDIFW KNCVGQERCG VSVVPEIFGG DPCPGTMKRA VVEAICG
//