ID BGAL6_ORYSJ Reviewed; 858 AA. AC Q10NX8; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 2. DT 27-MAR-2024, entry version 104. DE RecName: Full=Beta-galactosidase 6; DE Short=Lactase 6; DE EC=3.2.1.23; DE Flags: Precursor; GN OrderedLocusNames=Os03g0255100, LOC_Os03g15020; 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=16109971; DOI=10.1101/gr.3869505; RG The rice chromosome 3 sequencing consortium; RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K., RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., RA Jin W., Lee H.R., Jiang J., Jackson S.; RT "Sequence, annotation, and analysis of synteny between rice chromosome 3 RT and diverged grass species."; RL Genome Res. 15:1284-1291(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=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 PROTEIN SEQUENCE OF 31-80 AND 453-498, FUNCTION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RC STRAIN=cv. Nipponbare; TISSUE=Callus; RX PubMed=12723614; DOI=10.1271/bbb.67.627; RA Kaneko S., Kobayashi H.; RT "Purification and characterization of extracellular beta-galactosidase RT secreted by supension cultured rice (Oryza sativa L.) cells."; RL Biosci. Biotechnol. Biochem. 67:627-630(2003). CC -!- FUNCTION: Releases galactose by hydrolysis of plant cell wall CC galactose-containing polysaccharides such as galacto-xyloglucan, pectic CC galactan and galactan (in vitro). {ECO:0000269|PubMed:12723614}. 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 3.5. {ECO:0000269|PubMed:12723614}; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ABF95027.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=BAF11505.1; Type=Erroneous gene model prediction; Evidence={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; DP000009; ABF95027.1; ALT_SEQ; Genomic_DNA. DR EMBL; AP008209; BAF11505.1; ALT_SEQ; Genomic_DNA. DR EMBL; AP014959; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_015632058.1; XM_015776572.1. DR AlphaFoldDB; Q10NX8; -. DR SMR; Q10NX8; -. DR STRING; 39947.Q10NX8; -. DR CAZy; GH35; Glycoside Hydrolase Family 35. DR PaxDb; 39947-Q10NX8; -. DR GeneID; 4332289; -. DR KEGG; osa:4332289; -. DR eggNOG; KOG0496; Eukaryota. DR InParanoid; Q10NX8; -. DR OrthoDB; 5489808at2759; -. DR Proteomes; UP000000763; Chromosome 3. DR Proteomes; UP000059680; Chromosome 3. 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:SF124; BETA-GALACTOSIDASE 2-RELATED; 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. DR Genevisible; Q10NX8; OS. PE 1: Evidence at protein level; KW Apoplast; Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..30 FT /evidence="ECO:0000269|PubMed:12723614" FT CHAIN 31..858 FT /note="Beta-galactosidase 6" FT /id="PRO_0000294158" FT DOMAIN 772..858 FT /note="SUEL-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260" FT ACT_SITE 189 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 258 FT /note="Nucleophile" FT /evidence="ECO:0000255" FT CARBOHYD 32 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 259 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 482 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 507 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 595 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 830 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 79 FT /note="I -> F (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 858 AA; 92840 MW; DBD15B3FB1FF8067 CRC64; MAAATVGVLL RLLLLPVVVV VSLLVGASRA ANVTYDHRAV VIDGVRRVLV SGSIHYPRST PDMWPGLIQK SKDGGLDVIE TYVFWDIHEA VRGQYDFEGR KDLVRFVKAV ADAGLYVHLR IGPYVCAEWN YGGFPVWLHF VPGIKFRTDN EAFKAEMQRF TEKVVDTMKG AGLYASQGGP IILSQIENEY GNIDSAYGAA GKAYMRWAAG MAVSLDTGVP WVMCQQSDAP DPLINTCNGF YCDQFTPNSK SKPKMWTENW SGWFLSFGGA VPYRPAEDLA FAVARFYQRG GTFQNYYMYH GGTNFGRSTG GPFIATSYDY DAPIDEYGMV RQPKWGHLRD VHKAIKLCEP ALIAAEPSYS SLGQNTEATV YQTADNSICA AFLANVDAQS DKTVKFNGNT YKLPAWSVSI LPDCKNVVLN TAQINSQVTT SEMRSLGSSI QDTDDSLITP ELATAGWSYA IEPVGITKEN ALTKPGLMEQ INTTADASDF LWYSTSIVVK GDEPYLNGSQ SNLLVNSLGH VLQIYINGKL AGSAKGSASS SLISLQTPVT LVPGKNKIDL LSTTVGLSNY GAFFDLVGAG VTGPVKLSGP NGALNLSSTD WTYQIGLRGE DLHLYNPSEA SPEWVSDNAY PTNQPLIWYK TKFTAPAGDD PVAIDFTGMG KGEAWVNGQS IGRYWPTNLA PQSGCVNSCN YRGAYSSNKC LKKCGQPSQT LYHVPRSFLQ PGSNDLVLFE QFGGDPSMIS FTTRQTSSIC AHVSEMHPAQ IDSWISPQQT SQTQGPALRL ECPREGQVIS NIKFASFGTP SGTCGNYNHG ECSSSQALAV VQEACVGMTN CSVPVSSNNF GDPCSGVTKS LVVEAACS //