ID   BGAL7_ORYSJ             Reviewed;         775 AA.
AC   Q75HQ3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Beta-galactosidase 7;
DE            Short=Lactase 7;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os05g0428100, LOC_Os05g35360;
GN   ORFNames=OsJ_017861, OSJNBa0044P19.21, P0636F09.15;
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
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=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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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; AC135419; AAV25023.1; -; Genomic_DNA.
DR   EMBL; AC135429; AAS90664.1; -; Genomic_DNA.
DR   EMBL; AP014961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q75HQ3; -.
DR   SMR; Q75HQ3; -.
DR   STRING; 4530.OS05T0428100-00; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; Q75HQ3; -.
DR   PRIDE; Q75HQ3; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   InParanoid; Q75HQ3; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000007752; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
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   Gene3D; 2.60.120.740; -; 1.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
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; PTHR23421; 2.
DR   Pfam; PF13364; BetaGal_dom4_5; 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; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   3: Inferred from homology;
KW   Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..775
FT                   /note="Beta-galactosidase 7"
FT                   /id="PRO_0000294159"
FT   DOMAIN          689..775
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   ACT_SITE        185
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        256
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        602
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   775 AA;  86255 MW;  498AF4EDDFA324AB CRC64;
     MRGGMAITAA LVVVAAAAES RWAELGREIT YDGRALVVSG ARRMFFSGDM HYARSTPEMW
     PKLIAKAKNG GLDVIQTYVF WNVHEPIQGQ YNFEGRYDLV KFIREIQAQG LYVSLRIGPF
     VEAEWKYGGF PFWLHDVPSI TFRSDNEPFK QHMQNFVTKI VTMMKHEGLY YPQGGPIIIS
     QIENEYQMIE PAFGASGPRY VRWAAAMAVG LQTGVPWMMC KQNDAPDPVI NTCNGLICGE
     TFVGPNSPNK PALWTENWTS RSNGQNNSAF SYPIYGNDTK LRAPEDIAFA VALFIARKKG
     SFVSYYMYHG GTNFGRFAAS YVTTSYYDGA PLDEYDFKCV AFLVNFDQHN TPKVEFRNIS
     LELAPKSISV LSDCRNVVFE TAKVNAQHGS RTANAVQSLN DINNWKAFIE PVPQDLSKST
     YTGNQLFEQL TTTKDETDYL WYIVSYKNRA SDGNQIAHLY VKSLAHILHA FVNNEYVGSV
     HGSHDGPRNI VLNTHMSLKE GDNTISLLSV MVGSPDSGAY MERRTFGIQT VGIQQGQQPM
     HLLNNDLWGY QVGLFGEKDS IYTQEGTNSV RWMDINNLIY HPLTWYKTTF STPPGNDAVT
     LNLTSMGKGE VWVNGESIGR YWVSFKAPSG QPSQSLYHIP RGFLTPKDNL LVLVEEMGGD
     PLQITVNTMS VTTVCGNVDE FSVPPLQSRG KVPKVRIWCQ GGNRISSIEF ASYGNPVGDC
     RSFRIGSCHA ESSESVVKQS CIGRRGCSIP VMAAKFGGDP CPGIQKSLLV VADCR