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}.
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; 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 Genevisible; Q9SCV3; AT.
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.
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
//
