BGAL8_ARATH
ID BGAL8_ARATH Reviewed; 852 AA.
AC Q9SCV4; Q96257; Q9SK11;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Beta-galactosidase 8;
DE Short=Lactase 8;
DE EC=3.2.1.23;
DE AltName: Full=Protein AR782;
DE Flags: Precursor;
GN Name=BGAL8; OrderedLocusNames=At2g28470; ORFNames=T17D12.3;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [MRNA] OF 647-852.
RX PubMed=9287109; DOI=10.1016/s0014-5793(97)00871-5;
RA Hirayama T., Ishida C., Kuromori T., Obata S., Shimoda C., Yamamoto M.,
RA Shinozaki K., Ohto C.;
RT "Functional cloning of a cDNA encoding Mei2-like protein from Arabidopsis
RT thaliana using a fission yeast pheromone receptor deficient mutant.";
RL FEBS Lett. 413:16-20(1997).
RN [5]
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 [6]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SCV4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers and siliques.
CC {ECO:0000269|PubMed:16267099, ECO:0000269|PubMed:17466346}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21482.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ270304; CAB64744.1; -; mRNA.
DR EMBL; AC006587; AAD21482.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08127.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62009.1; -; Genomic_DNA.
DR EMBL; D88744; BAA13685.1; -; mRNA.
DR PIR; C84685; C84685.
DR RefSeq; NP_001324192.1; NM_001336165.1. [Q9SCV4-1]
DR RefSeq; NP_850121.1; NM_179790.3. [Q9SCV4-1]
DR AlphaFoldDB; Q9SCV4; -.
DR SMR; Q9SCV4; -.
DR STRING; 3702.AT2G28470.1; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; Q9SCV4; -.
DR PRIDE; Q9SCV4; -.
DR ProteomicsDB; 240654; -. [Q9SCV4-1]
DR EnsemblPlants; AT2G28470.1; AT2G28470.1; AT2G28470. [Q9SCV4-1]
DR EnsemblPlants; AT2G28470.3; AT2G28470.3; AT2G28470. [Q9SCV4-1]
DR GeneID; 817395; -.
DR Gramene; AT2G28470.1; AT2G28470.1; AT2G28470. [Q9SCV4-1]
DR Gramene; AT2G28470.3; AT2G28470.3; AT2G28470. [Q9SCV4-1]
DR KEGG; ath:AT2G28470; -.
DR Araport; AT2G28470; -.
DR TAIR; locus:2056623; AT2G28470.
DR eggNOG; KOG0496; Eukaryota.
DR InParanoid; Q9SCV4; -.
DR OrthoDB; 179316at2759; -.
DR PhylomeDB; Q9SCV4; -.
DR BioCyc; ARA:AT2G28470-MON; -.
DR PRO; PR:Q9SCV4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SCV4; baseline and differential.
DR Genevisible; Q9SCV4; 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 Alternative splicing; Apoplast; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..852
FT /note="Beta-galactosidase 8"
FT /id="PRO_5000065882"
FT DOMAIN 766..852
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 568
FT /note="V -> M (in Ref. 1; CAB64744)"
FT /evidence="ECO:0000305"
FT CONFLICT 647..648
FT /note="FT -> TA (in Ref. 4; BAA13685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 93210 MW; 54DCFB09790EE045 CRC64;
MEIAAKMVKV RKMEMILLLI LVIVVAATAA NVTYDHRALV IDGKRKVLIS GSIHYPRSTP
EMWPELIQKS KDGGLDVIET YVFWSGHEPE KNKYNFEGRY DLVKFVKLAA KAGLYVHLRI
GPYVCAEWNY GGFPVWLHFV PGIKFRTDNE PFKEEMQRFT TKIVDLMKQE KLYASQGGPI
ILSQIENEYG NIDSAYGAAA KSYIKWSASM ALSLDTGVPW NMCQQTDAPD PMINTCNGFY
CDQFTPNSNN KPKMWTENWS GWFLGFGDPS PYRPVEDLAF AVARFYQRGG TFQNYYMYHG
GTNFDRTSGG PLISTSYDYD APIDEYGLLR QPKWGHLRDL HKAIKLCEDA LIATDPTITS
LGSNLEAAVY KTESGSCAAF LANVDTKSDA TVTFNGKSYN LPAWSVSILP DCKNVAFNTA
KINSATESTA FARQSLKPDG GSSAELGSQW SYIKEPIGIS KADAFLKPGL LEQINTTADK
SDYLWYSLRT DIKGDETFLD EGSKAVLHIE SLGQVVYAFI NGKLAGSGHG KQKISLDIPI
NLVTGTNTID LLSVTVGLAN YGAFFDLVGA GITGPVTLKS AKGGSSIDLA SQQWTYQVGL
KGEDTGLATV DSSEWVSKSP LPTKQPLIWY KTTFDAPSGS EPVAIDFTGT GKGIAWVNGQ
SIGRYWPTSI AGNGGCTESC DYRGSYRANK CLKNCGKPSQ TLYHVPRSWL KPSGNILVLF
EEMGGDPTQI SFATKQTGSN LCLTVSQSHP PPVDTWTSDS KISNRNRTRP VLSLKCPIST
QVIFSIKFAS FGTPKGTCGS FTQGHCNSSR SLSLVQKACI GLRSCNVEVS TRVFGEPCRG
VVKSLAVEAS CS
