ID BGA10_ARATH Reviewed; 741 AA.
AC Q9FN08; Q9SCV2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 133.
DE RecName: Full=Beta-galactosidase 10;
DE Short=Lactase 10;
DE EC=3.2.1.23;
DE Flags: Precursor;
GN Name=BGAL10; OrderedLocusNames=At5g63810; ORFNames=MGI19.1;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 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 -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16267099,
CC ECO:0000269|PubMed:17466346}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; AJ270306; CAB64746.1; -; mRNA.
DR EMBL; AB007646; BAB11029.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97800.1; -; Genomic_DNA.
DR EMBL; AY093118; AAM13117.1; -; mRNA.
DR EMBL; BT010338; AAQ56781.1; -; mRNA.
DR RefSeq; NP_201186.1; NM_125776.2.
DR AlphaFoldDB; Q9FN08; -.
DR SMR; Q9FN08; -.
DR STRING; 3702.Q9FN08; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR GlyCosmos; Q9FN08; 6 sites, No reported glycans.
DR PaxDb; 3702-AT5G63810-1; -.
DR ProteomicsDB; 240417; -.
DR EnsemblPlants; AT5G63810.1; AT5G63810.1; AT5G63810.
DR GeneID; 836501; -.
DR Gramene; AT5G63810.1; AT5G63810.1; AT5G63810.
DR KEGG; ath:AT5G63810; -.
DR Araport; AT5G63810; -.
DR TAIR; AT5G63810; BGAL10.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q9FN08; -.
DR OMA; NGTHSPF; -.
DR OrthoDB; 5489808at2759; -.
DR PhylomeDB; Q9FN08; -.
DR BioCyc; ARA:AT5G63810-MONOMER; -.
DR PRO; PR:Q9FN08; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN08; baseline and differential.
DR Genevisible; Q9FN08; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004565; F:beta-galactosidase activity; IMP:CACAO.
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:SF67; BETA-GALACTOSIDASE 10; 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.
PE 2: Evidence at transcript level;
KW Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..741
FT /note="Beta-galactosidase 10"
FT /id="PRO_5000065884"
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 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 544
FT /note="N -> T (in Ref. 1; CAB64746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 83102 MW; 6BEE67970375CE98 CRC64;
MNRVTTESIA STAILVVMVF LFSWRSIEAA NVSYDHRSLT IGNRRQLIIS AAIHYPRSVP
AMWPSLVQTA KEGGCNAIES YVFWNGHEPS PGKYYFGGRY NIVKFIKIVQ QAGMHMILRI
GPFVAAEWNY GGVPVWLHYV PGTVFRADNE PWKHYMESFT TYIVNLLKQE KLFAPQGGPI
ILSQVENEYG YYEKDYGEGG KRYAQWSASM AVSQNIGVPW MMCQQWDAPP TVISTCNGFY
CDQFTPNTPD KPKIWTENWP GWFKTFGGRD PHRPAEDVAY SVARFFGKGG SVHNYYMYHG
GTNFGRTSGG PFITTSYDYE APIDEYGLPR LPKWGHLKDL HKAIMLSENL LISGEHQNFT
LGHSLEADVY TDSSGTCAAF LSNLDDKNDK AVMFRNTSYH LPAWSVSILP DCKTEVFNTA
KVTSKSSKVE MLPEDLKSSS GLKWEVFSEK PGIWGAADFV KNELVDHINT TKDTTDYLWY
TTSITVSENE AFLKKGSSPV LFIESKGHTL HVFINKEYLG TATGNGTHVP FKLKKPVALK
AGENNIDLLS MTVGLANAGS FYEWVGAGLT SVSIKGFNKG TLNLTNSKWS YKLGVEGEHL
ELFKPGNSGA VKWTVTTKPP KKQPLTWYKV VIEPPSGSEP VGLDMISMGK GMAWLNGEEI
GRYWPRIARK NSPNDECVKE CDYRGKFMPD KCLTGCGEPS QRWYHVPRSW FKSSGNELVI
FEEKGGNPMK IKLSKRKVSV V
//
