ID   BGA11_ARATH             Reviewed;         845 AA.
AC   Q9SCV1; O49609;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 139.
DE   RecName: Full=Beta-galactosidase 11;
DE            Short=Lactase 11;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   Name=BGAL11; OrderedLocusNames=At4g35010; ORFNames=M4E13.70;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA17766.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80218.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ270307; CAB64747.1; -; mRNA.
DR   EMBL; AL022023; CAA17766.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161586; CAB80218.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86446.1; -; Genomic_DNA.
DR   PIR; T05771; T05771.
DR   RefSeq; NP_567973.1; NM_119667.3.
DR   AlphaFoldDB; Q9SCV1; -.
DR   SMR; Q9SCV1; -.
DR   STRING; 3702.Q9SCV1; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; Q9SCV1; 7 sites, No reported glycans.
DR   PaxDb; 3702-AT4G35010-1; -.
DR   ProteomicsDB; 240655; -.
DR   EnsemblPlants; AT4G35010.1; AT4G35010.1; AT4G35010.
DR   GeneID; 829653; -.
DR   Gramene; AT4G35010.1; AT4G35010.1; AT4G35010.
DR   KEGG; ath:AT4G35010; -.
DR   Araport; AT4G35010; -.
DR   TAIR; AT4G35010; BGAL11.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   InParanoid; Q9SCV1; -.
DR   OMA; QVIEKHC; -.
DR   OrthoDB; 1204541at2759; -.
DR   PhylomeDB; Q9SCV1; -.
DR   BioCyc; ARA:AT4G35010-MONOMER; -.
DR   PRO; PR:Q9SCV1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SCV1; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; TAS:TAIR.
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; IPR025300; BetaGal_jelly_roll_dom.
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:SF130; BETA-GALACTOSIDASE 11; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF13364; BetaGal_ABD2; 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; Q9SCV1; AT.
PE   2: Evidence at transcript level;
KW   Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..845
FT                   /note="Beta-galactosidase 11"
FT                   /id="PRO_0000293093"
FT   DOMAIN          751..840
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   ACT_SITE        197
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        268
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        752
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        784
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        814
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   845 AA;  95570 MW;  EAD24C68E0097B2D CRC64;
     MRKHSLDRWL LTAVLVVLLS SSSSFAAKKD AKKKKKSNKE VTYDGTSLII DGKRELLYSG
     SIHYPRSTPE MWPSIIKRAK QGGLNTIQTY VFWNVHEPQQ GKFNFSGRAD LVKFIKLIQK
     NGMYVTLRLG PFIQAEWTHG GLPYWLREVP GIFFRTDNKQ FKEHTERYVR MILDKMKEER
     LFASQGGPII LGQIENEYSA VQRAYKQDGL NYIKWASNLV DSMKLGIPWV MCKQNDAPDP
     MINACNGRHC GDTFPGPNRE NKPSLWTENW TTQFRVFGDP PTQRSVEDIA YSVARFFSKN
     GTHVNYYMYH GGTNFGRTSA HYVTTRYYDD APLDEYGLEK EPKYGHLKHL HNALNLCKKP
     LLWGQPKTEK PGKDTEIRYY EQPGTKTCAA FLANNNTEAA ETIKFKGREY VIAPRSISIL
     PDCKTVVYNT AQIVSQHTSR NFMKSKKANK KFDFKVFTET LPSKLEGNSY IPVELYGLTK
     DKTDYGWYTT SFKVHKNHLP TKKGVKTFVR IASLGHALHA WLNGEYLGSG HGSHEEKSFV
     FQKQVTLKAG ENHLVMLGVL TGFPDSGSYM EHRYTGPRGI SILGLTSGTL DLTESSKWGN
     KIGMEGEKLG IHTEEGLKKV EWKKFTGKAP GLTWYQTYFD APESVSAATI RMHGMGKGLI
     WVNGEGVGRY WQSFLSPLGQ PTQIEYHIPR SFLKPKKNLL VIFEEEPNVK PELMDFAIVN
     RDTVCSYVGE NYTPSVRHWT RKKDQVQAIT DNVSLTATLK CSGTKKIAAV EFASFGNPIG
     VCGNFTLGTC NAPVSKQVIE KHCLGKAECV IPVNKSTFQQ DKKDSCKNVV KMLAVQVKCG
     RGKKN
//