ID   BGAL9_ARATH             Reviewed;         887 AA.
AC   Q9SCV3; O48836;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Beta-galactosidase 9;
DE            Short=Lactase 9;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   Name=BGAL9; OrderedLocusNames=At2g32810; ORFNames=F24L7.5;
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   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   [5]
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=Q9SCV3-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with higher expression levels in
CC       siliques. {ECO:0000269|PubMed:16267099, ECO:0000269|PubMed:17466346}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; AJ270305; CAB64745.1; -; mRNA.
DR   EMBL; AC003974; AAC04500.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08744.1; -; Genomic_DNA.
DR   PIR; T00787; T00787.
DR   RefSeq; NP_565755.1; NM_128841.5. [Q9SCV3-1]
DR   AlphaFoldDB; Q9SCV3; -.
DR   SMR; Q9SCV3; -.
DR   BioGRID; 3189; 1.
DR   STRING; 3702.Q9SCV3; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; Q9SCV3; 7 sites, No reported glycans.
DR   PaxDb; 3702-AT2G32810-1; -.
DR   ProteomicsDB; 240677; -. [Q9SCV3-1]
DR   EnsemblPlants; AT2G32810.1; AT2G32810.1; AT2G32810. [Q9SCV3-1]
DR   GeneID; 817842; -.
DR   Gramene; AT2G32810.1; AT2G32810.1; AT2G32810. [Q9SCV3-1]
DR   KEGG; ath:AT2G32810; -.
DR   Araport; AT2G32810; -.
DR   TAIR; AT2G32810; BGAL9.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_1_1; -.
DR   InParanoid; Q9SCV3; -.
DR   OMA; NFFEPFN; -.
DR   OrthoDB; 5489808at2759; -.
DR   PhylomeDB; Q9SCV3; -.
DR   BioCyc; ARA:AT2G32810-MONOMER; -.
DR   PRO; PR:Q9SCV3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SCV3; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd22842; Gal_Rha_Lectin_BGal; 1.
DR   Gene3D; 2.60.120.740; -; 1.
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   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   PANTHER; PTHR23421:SF13; BETA-GALACTOSIDASE 9; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 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; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
DR   Genevisible; Q9SCV3; AT.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoplast; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..887
FT                   /note="Beta-galactosidase 9"
FT                   /id="PRO_5000065883"
FT   DOMAIN          791..877
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   ACT_SITE        194
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        463
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        496
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        527
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        785
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        881
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   887 AA;  99199 MW;  51FC80516B1C85EC CRC64;
     MAESIRTFSL QWRILSLIIA LLVYFPILSG SYFKPFNVSY DHRALIIAGK RRMLVSAGIH
     YPRATPEMWS DLIAKSKEGG ADVVQTYVFW NGHEPVKGQY NFEGRYDLVK FVKLIGSSGL
     YLHLRIGPYV CAEWNFGGFP VWLRDIPGIE FRTDNEPFKK EMQKFVTKIV DLMREAKLFC
     WQGGPIIMLQ IENEYGDVEK SYGQKGKDYV KWAASMALGL GAGVPWVMCK QTDAPENIID
     ACNGYYCDGF KPNSRTKPVL WTEDWDGWYT KWGGSLPHRP AEDLAFAVAR FYQRGGSFQN
     YYMYFGGTNF GRTSGGPFYI TSYDYDAPLD EYGLRSEPKW GHLKDLHAAI KLCEPALVAA
     DAPQYRKLGS KQEAHIYHGD GETGGKVCAA FLANIDEHKS AHVKFNGQSY TLPPWSVSIL
     PDCRHVAFNT AKVGAQTSVK TVESARPSLG SMSILQKVVR QDNVSYISKS WMALKEPIGI
     WGENNFTFQG LLEHLNVTKD RSDYLWHKTR ISVSEDDISF WKKNGPNSTV SIDSMRDVLR
     VFVNKQLAGS IVGHWVKAVQ PVRFIQGNND LLLLTQTVGL QNYGAFLEKD GAGFRGKAKL
     TGFKNGDLDL SKSSWTYQVG LKGEADKIYT VEHNEKAEWS TLETDASPSI FMWYKTYFDP
     PAGTDPVVLN LESMGRGQAW VNGQHIGRYW NIISQKDGCD RTCDYRGAYN SDKCTTNCGK
     PTQTRYHVPR SWLKPSSNLL VLFEETGGNP FKISVKTVTA GILCGQVSES HYPPLRKWST
     PDYINGTMSI NSVAPEVHLH CEDGHVISSI EFASYGTPRG SCDGFSIGKC HASNSLSIVS
     EACKGRNSCF IEVSNTAFIS DPCSGTLKTL AVMSRCSPSQ NMSDLSF
//