ID   BGAL2_ARATH             Reviewed;         727 AA.
AC   Q9LFA6; Q8H7H7; Q9SCW0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=Beta-galactosidase 2;
DE            Short=Lactase 2;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   Name=BGAL2; OrderedLocusNames=At3g52840; ORFNames=F8J2.10;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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 1-569.
RA   Stracke R., Palme K.;
RT   "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT   and guard cells.";
RL   Submitted (AUG-1998) 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).
RN   [8]
RP   INDUCTION.
RX   PubMed=17234672; DOI=10.1093/pcp/pcm009;
RA   Lee E.-J., Matsumura Y., Soga K., Hoson T., Koizumi N.;
RT   "Glycosyl hydrolases of cell wall are induced by sugar starvation in
RT   Arabidopsis.";
RL   Plant Cell Physiol. 48:405-413(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, with higher expression levels in roots
CC       and siliques. {ECO:0000269|PubMed:16267099,
CC       ECO:0000269|PubMed:17466346}.
CC   -!- INDUCTION: By sugar starvation. {ECO:0000269|PubMed:17234672}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; AJ270298; CAB64738.1; -; mRNA.
DR   EMBL; AL132969; CAB86888.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78999.1; -; Genomic_DNA.
DR   EMBL; AF367327; AAK32914.1; -; mRNA.
DR   EMBL; BT000511; AAN18080.1; -; mRNA.
DR   EMBL; AF083670; AAN60229.1; -; mRNA.
DR   PIR; T47541; T47541.
DR   RefSeq; NP_190852.2; NM_115144.4.
DR   AlphaFoldDB; Q9LFA6; -.
DR   SMR; Q9LFA6; -.
DR   STRING; 3702.Q9LFA6; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; Q9LFA6; 1 site, No reported glycans.
DR   PaxDb; 3702-AT3G52840-1; -.
DR   ProteomicsDB; 240658; -.
DR   EnsemblPlants; AT3G52840.1; AT3G52840.1; AT3G52840.
DR   GeneID; 824450; -.
DR   Gramene; AT3G52840.1; AT3G52840.1; AT3G52840.
DR   KEGG; ath:AT3G52840; -.
DR   Araport; AT3G52840; -.
DR   TAIR; AT3G52840; BGAL2.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   InParanoid; Q9LFA6; -.
DR   OMA; YPAKVMF; -.
DR   BRENDA; 3.2.1.23; 399.
DR   PRO; PR:Q9LFA6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LFA6; baseline and differential.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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   PANTHER; PTHR23421:SF194; BETA-GALACTOSIDASE 2; 1.
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   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   Genevisible; Q9LFA6; AT.
PE   2: Evidence at transcript level;
KW   Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..727
FT                   /note="Beta-galactosidase 2"
FT                   /id="PRO_5000065878"
FT   ACT_SITE        185
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        254
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        12
FT                   /note="I -> F (in Ref. 5; AAN60229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220
FT                   /note="C -> S (in Ref. 2; CAB86888)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   727 AA;  82015 MW;  21FF54744E67F5C5 CRC64;
     MSMHFRNKAW IILAILCFSS LIHSTEAVVT YDHKALIING QRRILISGSI HYPRSTPEMW
     PDLIKKAKEG GLDVIQTYVF WNGHEPSPGN YYFQDRYDLV KFTKLVHQAG LYLDLRIGPY
     VCAEWNFGGF PVWLKYVPGM VFRTDNEPFK IAMQKFTKKI VDMMKEEKLF ETQGGPIILS
     QIENEYGPMQ WEMGAAGKAY SKWTAEMALG LSTGVPWIMC KQEDAPYPII DTCNGFYCEG
     FKPNSDNKPK LWTENWTGWF TEFGGAIPNR PVEDIAFSVA RFIQNGGSFM NYYMYYGGTN
     FDRTAGVFIA TSYDYDAPID EYGLLREPKY SHLKELHKVI KLCEPALVSV DPTITSLGDK
     QEIHVFKSKT SCAAFLSNYD TSSAARVMFR GFPYDLPPWS VSILPDCKTE YYNTAKIRAP
     TILMKMIPTS TKFSWESYNE GSPSSNEAGT FVKDGLVEQI SMTRDKTDYF WYFTDITIGS
     DESFLKTGDN PLLTIFSAGH ALHVFVNGLL AGTSYGALSN SKLTFSQNIK LSVGINKLAL
     LSTAVGLPNA GVHYETWNTG ILGPVTLKGV NSGTWDMSKW KWSYKIGLRG EAMSLHTLAG
     SSAVKWWIKG FVVKKQPLTW YKSSFDTPRG NEPLALDMNT MGKGQVWVNG HNIGRHWPAY
     TARGNCGRCN YAGIYNEKKC LSHCGEPSQR WYHVPRSWLK PFGNLLVIFE EWGGDPSGIS
     LVKRTAK
//