ID BGAL7_ARATH Reviewed; 826 AA. AC Q9SCV5; Q94AU4; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 2. DT 04-NOV-2026, entry version 148. DE RecName: Full=Beta-galactosidase 7; DE Short=Lactase 7; DE EC=3.2.1.23; DE Flags: Precursor; GN Name=BGAL7; OrderedLocusNames=At5g20710; ORFNames=T1M15.110; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130714; DOI=10.1038/35048507; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., RA Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."; RL Nature 408:823-826(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-826. RA Gy I., Kreis M., Lecharny A.; RT "The beta-galactosidases are encoding by a multigene family in Arabidopsis RT thaliana."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-826. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE. RX PubMed=17466346; DOI=10.1016/j.phytochem.2007.03.021; RA Ahn Y.O., Zheng M., Bevan D.R., Esen A., Shiu S.-H., Benson J., Peng H.-P., RA Miller J.T., Cheng C.-L., Poulton J.E., Shih M.-C.; RT "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase RT family 35."; RL Phytochemistry 68:1510-1520(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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast CC {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in flowers. CC {ECO:0000269|PubMed:17466346}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK76465.1; Type=Erroneous initiation; 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; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CP002688; AED92880.1; -; Genomic_DNA. DR EMBL; OZ408687; CAO7053020.1; -; Genomic_DNA. DR EMBL; AJ270303; CAB64743.1; -; mRNA. DR EMBL; AY045791; AAK76465.1; ALT_INIT; mRNA. DR RefSeq; NP_568399.4; NM_122078.5. DR AlphaFoldDB; Q9SCV5; -. DR SMR; Q9SCV5; -. DR FunCoup; Q9SCV5; 1. DR STRING; 3702.Q9SCV5; -. DR GlyCosmos; Q9SCV5; 9 sites, No reported glycans. DR GlyGen; Q9SCV5; 9 sites. DR PaxDb; 3702-Q9SCV5; -. DR ProteomicsDB; 240855; -. DR GeneID; 832194; -. DR KEGG; ath:AT5G20710; -. DR Araport; AT5G20710; -. DR TAIR; AT5G20710; BGAL7. DR eggNOG; KOG0496; Eukaryota. DR HOGENOM; CLU_007853_4_0_1; -. DR InParanoid; Q9SCV5; -. DR OMA; ACSEDRV; -. DR PhylomeDB; Q9SCV5; -. DR BioCyc; ARA:AT5G20710-MONOMER; -. DR PRO; PR:Q9SCV5; -. DR Proteomes; UP000006548; Chromosome 5. DR Proteomes; UP001984100; Chromosome 5. DR ExpressionAtlas; Q9SCV5; baseline and differential. DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; ISM:TAIR. DR GO; GO:0009505; C:plant-type cell wall; 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:0019388; P:galactose catabolic process; IBA:GO_Central. DR GO; GO:0009827; P:plant-type cell wall modification; IBA:GO_Central. DR CDD; cd22842; Gal_Rha_Lectin_BGal; 1. DR FunFam; 2.60.120.260:FF:000097; Beta-galactosidase; 1. DR FunFam; 2.60.120.260:FF:000142; Beta-galactosidase; 1. DR FunFam; 3.20.20.80:FF:000267; Beta-galactosidase; 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; IPR017853; GH_hydrolase_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; IPR000922; Lectin_gal-bd_dom. DR InterPro; IPR043159; Lectin_gal-bd_sf. DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1. DR Pfam; PF21467; BetaGal_gal-bd; 1. DR Pfam; PF17834; GHD; 1. DR Pfam; PF01301; Glyco_hydro_35; 1. DR Pfam; PF02140; SUEL_Lectin; 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 2: Evidence at transcript level; KW Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..826 FT /note="Beta-galactosidase 7" FT /id="PRO_0000293092" FT DOMAIN 740..826 FT /note="SUEL-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260" FT ACT_SITE 184 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 253 FT /note="Nucleophile" FT /evidence="ECO:0000255" FT CARBOHYD 154 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 254 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 351 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 380 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 491 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 665 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 706 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 797 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 801 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 674 FT /note="E -> K (in Ref. 5; AAK76465)" FT /evidence="ECO:0000305" SQ SEQUENCE 826 AA; 92712 MW; 3EDA7EBA3E5D234B CRC64; MKMKHFTRLL SLFFILITSL SLAKSTIVSH DERAITINGK RRILLSGSIH YPRSTADMWP DLINKAKDGG LDAIETYVFW NAHEPKRREY DFSGNLDVVR FIKTIQDAGL YSVLRIGPYV CAEWNYGGFP VWLHNMPNMK FRTVNPSFMN EMQNFTTKIV KMMKEEKLFA SQGGPIILAQ IENEYGNVIS SYGAEGKAYI DWCANMANSL DIGVPWLMCQ QPNAPQPMLE TCNGFYCDQY EPTNPSTPKM WTENWTGWFK NWGGKHPYRT AEDLAFSVAR FFQTGGTFQN YYMYHGGTNF GRVAGGPYIT TSYDYHAPLD EFGNLNQPKW GHLKQLHTVL KSMEKSLTYG NISRIDLGNS IKATIYTTKE GSSCFIGNVN ATADALVNFK GKDYHVPAWS VSVLPDCDKE AYNTAKVNTQ TSIMTEDSSK PERLEWTWRP ESAQKMILKG SGDLIAKGLV DQKDVTNDAS DYLWYMTRLH LDKKDPLWSR NMTLRVHSNA HVLHAYVNGK YVGNQFVKDG KFDYRFERKV NHLVHGTNHI SLLSVSVGLQ NYGPFFESGP TGINGPVSLV GYKGEETIEK DLSQHQWDYK IGLNGYNDKL FSIKSVGHQK WANEKLPTGR MLTWYKAKFK APLGKEPVIV DLNGLGKGEA WINGQSIGRY WPSFNSSDDG CKDECDYRGA YGSDKCAFMC GKPTQRWYHV PRSFLNASGH NTITLFEEMG GNPSMVNFKT VVVGTVCARA HEHNKVELSC HNRPISAVKF ASFGNPLGHC GSFAVGTCQG DKDAAKTVAK ECVGKLNCTV NVSSDTFGST LDCGDSPKKL AVELEC //