ID   BGAL1_ARATH             Reviewed;         847 AA.
AC   Q9SCW1; Q56W18; Q8RWC1;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 166.
DE   RecName: Full=Beta-galactosidase 1;
DE            Short=Lactase 1;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   Name=BGAL1; OrderedLocusNames=At3g13750; ORFNames=MMM17.1;
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 [MRNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 578-847.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=16267099; DOI=10.1093/pcp/pci223;
RA   Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I.;
RT   "Apoplastic glycosidases active against xyloglucan oligosaccharides of
RT   Arabidopsis thaliana.";
RL   Plant Cell Physiol. 47:55-63(2006).
RN   [8]
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: Ubiquitous, at low levels.
CC       {ECO:0000269|PubMed:16267099, ECO:0000269|PubMed:17466346}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; AJ270297; CAB64737.1; -; mRNA.
DR   EMBL; AP001307; BAB01923.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75407.1; -; Genomic_DNA.
DR   EMBL; OZ408685; CAO7040803.1; -; Genomic_DNA.
DR   EMBL; AY093197; AAM13196.1; -; mRNA.
DR   EMBL; AK222229; BAD95407.1; -; mRNA.
DR   RefSeq; NP_187988.1; NM_112225.5.
DR   AlphaFoldDB; Q9SCW1; -.
DR   SMR; Q9SCW1; -.
DR   BioGRID; 5918; 3.
DR   FunCoup; Q9SCW1; 308.
DR   IntAct; Q9SCW1; 1.
DR   STRING; 3702.Q9SCW1; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; Q9SCW1; 1 site, No reported glycans.
DR   GlyGen; Q9SCW1; 1 site.
DR   iPTMnet; Q9SCW1; -.
DR   PaxDb; 3702-Q9SCW1; -.
DR   ProteomicsDB; 240679; -.
DR   GeneID; 820584; -.
DR   KEGG; ath:AT3G13750; -.
DR   Araport; AT3G13750; -.
DR   TAIR; AT3G13750; BGAL1.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   InParanoid; Q9SCW1; -.
DR   OMA; NYDQHSF; -.
DR   PhylomeDB; Q9SCW1; -.
DR   BioCyc; ARA:AT3G13750-MONOMER; -.
DR   CD-CODE; 4299E36E; Nucleolus.
DR   PRO; PR:Q9SCW1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005576; C:extracellular region; ISM:TAIR.
DR   GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IDA:TAIR.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0019388; P:galactose catabolic process; IBA:GO_Central.
DR   CDD; cd22842; Gal_Rha_Lectin_BGal; 1.
DR   FunFam; 2.60.120.260:FF:000061; Beta-galactosidase; 1.
DR   FunFam; 2.60.120.260:FF:000076; Beta-galactosidase; 1.
DR   FunFam; 2.60.120.260:FF:000142; Beta-galactosidase; 1.
DR   FunFam; 2.60.120.740:FF:000002; Beta-galactosidase; 1.
DR   FunFam; 3.20.20.80:FF:000021; Beta-galactosidase; 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; 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; 2.
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; PS00435; PEROXIDASE_1; 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..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..847
FT                   /note="Beta-galactosidase 1"
FT                   /id="PRO_5000065877"
FT   DOMAIN          761..847
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   ACT_SITE        190
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        259
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        512
FT                   /note="V -> L (in Ref. 5; AAM13196)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   847 AA;  93659 MW;  91C13DE26A4CF4AD CRC64;
     MGSKPNAMKN VVAMAAVSAL FLLGFLVCSV SGSVSYDSRA ITINGKRRIL ISGSIHYPRS
     TPEMWPDLIR KAKEGGLDVI QTYVFWNGHE PSPGKYYFEG NYDLVKFVKL VQQSGLYLHL
     RIGPYVCAEW NFGGFPVWLK YIPGISFRTD NGPFKAQMQR FTTKIVNMMK AERLFESQGG
     PIILSQIENE YGPMEYELGA PGRSYTNWAA KMAVGLGTGV PWVMCKQDDA PDPIINACNG
     FYCDYFSPNK AYKPKMWTEA WTGWFTKFGG PVPYRPAEDM AFSVARFIQK GGSFINYYMY
     HGGTNFGRTA GGPFIATSYD YDAPLDEYGL ERQPKWGHLK DLHRAIKLCE PALVSGEPTR
     MPLGNYQEAH VYKSKSGACS AFLANYNPKS YAKVSFGNNH YNLPPWSISI LPDCKNTVYN
     TARVGAQTSR MKMVRVPVHG GLSWQAYNED PSTYIDESFT MVGLVEQINT TRDTSDYLWY
     MTDVKVDANE GFLRNGDLPT LTVLSAGHAM HVFINGQLSG SAYGSLDSPK LTFRKGVNLR
     AGFNKIAILS IAVGLPNVGP HFETWNAGVL GPVSLNGLNG GRRDLSWQKW TYKVGLKGES
     LSLHSLSGSS SVEWAEGAFV AQKQPLTWYK TTFSAPAGDS PLAVDMGSMG KGQIWINGQS
     LGRHWPAYKA VGSCSECSYT GTFREDKCLR NCGEASQRWY HVPRSWLKPS GNLLVVFEEW
     GGDPNGITLV RREVDSVCAD IYEWQSTLVN YQLHASGKVN KPLHPKAHLQ CGPGQKITTV
     KFASFGTPEG TCGSYRQGSC HAHHSYDAFN KLCVGQNWCS VTVAPEMFGG DPCPNVMKKL
     AVEAVCA
//