BGAL1_ARATH
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 03-AUG-2022, entry version 150.
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 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 [5]
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 [6]
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 [7]
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; 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 IntAct; Q9SCW1; 1.
DR STRING; 3702.AT3G13750.1; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; Q9SCW1; -.
DR PRIDE; Q9SCW1; -.
DR ProteomicsDB; 240679; -.
DR EnsemblPlants; AT3G13750.1; AT3G13750.1; AT3G13750.
DR GeneID; 820584; -.
DR Gramene; AT3G13750.1; AT3G13750.1; AT3G13750.
DR KEGG; ath:AT3G13750; -.
DR Araport; AT3G13750; -.
DR TAIR; locus:2091496; AT3G13750.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q9SCW1; -.
DR OMA; AFSWQAY; -.
DR OrthoDB; 179316at2759; -.
DR PhylomeDB; Q9SCW1; -.
DR BioCyc; ARA:AT3G13750-MON; -.
DR PRO; PR:Q9SCW1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCW1; baseline and differential.
DR Genevisible; Q9SCW1; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA: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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.740; -; 1.
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; 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; 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. 4; 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
