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 24-JAN-2024, entry version 109. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 39947.Q75HQ3; -. DR CAZy; GH35; Glycoside Hydrolase Family 35. DR PaxDb; 39947-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 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; 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:SF190; BETA-GALACTOSIDASE 7; 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 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 //