BGAL2_ARATH
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 25-MAY-2022, entry version 130.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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.AT3G52840.1; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; Q9LFA6; -.
DR PRIDE; Q9LFA6; -.
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; locus:2085131; AT3G52840.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q9LFA6; -.
DR OMA; GTHYETW; -.
DR BRENDA; 3.2.1.23; 399.
DR PRO; PR:Q9LFA6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LFA6; baseline and differential.
DR Genevisible; Q9LFA6; AT.
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:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; PTHR23421; 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.
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
