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BGA10_ARATH
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   03-AUG-2022, entry version 127.
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.AT5G63810.1; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; Q9FN08; -.
DR   PRIDE; Q9FN08; -.
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; locus:2163951; AT5G63810.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   InParanoid; Q9FN08; -.
DR   OMA; HKSIKLG; -.
DR   OrthoDB; 179316at2759; -.
DR   PhylomeDB; Q9FN08; -.
DR   BioCyc; ARA:AT5G63810-MON; -.
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:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IMP:CACAO.
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..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
 
 
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