BGAL7_ARATH
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 03-AUG-2022, entry version 131.
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 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 [4]
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 [5]
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};
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DR EMBL; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92880.1; -; 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 STRING; 3702.AT5G20710.1; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; Q9SCV5; -.
DR PRIDE; Q9SCV5; -.
DR ProteomicsDB; 240855; -.
DR EnsemblPlants; AT5G20710.1; AT5G20710.1; AT5G20710.
DR GeneID; 832194; -.
DR Gramene; AT5G20710.1; AT5G20710.1; AT5G20710.
DR KEGG; ath:AT5G20710; -.
DR Araport; AT5G20710; -.
DR TAIR; locus:2180439; AT5G20710.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q9SCV5; -.
DR OMA; IQSAHEY; -.
DR OrthoDB; 179316at2759; -.
DR PhylomeDB; Q9SCV5; -.
DR BioCyc; ARA:AT5G20710-MON; -.
DR PRO; PR:Q9SCV5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SCV5; baseline and differential.
DR Genevisible; Q9SCV5; AT.
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 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; 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. 4; 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
