BGA13_ARATH
ID BGA13_ARATH Reviewed; 848 AA.
AC Q9SCU9; Q9SLE5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Beta-galactosidase 13;
DE Short=Lactase 13;
DE EC=3.2.1.23;
DE Flags: Precursor;
GN Name=BGAL13; OrderedLocusNames=At2g16730; ORFNames=T24I21.14;
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 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, with higher expression levels in roots,
CC flowers and siliques. {ECO:0000269|PubMed:16267099}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24606.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ270309; CAB64749.1; -; mRNA.
DR EMBL; AC005825; AAD24606.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06532.1; -; Genomic_DNA.
DR PIR; E84543; E84543.
DR RefSeq; NP_179264.2; NM_127225.3.
DR AlphaFoldDB; Q9SCU9; -.
DR SMR; Q9SCU9; -.
DR STRING; 3702.AT2G16730.1; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; Q9SCU9; -.
DR PRIDE; Q9SCU9; -.
DR ProteomicsDB; 240461; -.
DR EnsemblPlants; AT2G16730.1; AT2G16730.1; AT2G16730.
DR GeneID; 816174; -.
DR Gramene; AT2G16730.1; AT2G16730.1; AT2G16730.
DR KEGG; ath:AT2G16730; -.
DR Araport; AT2G16730; -.
DR TAIR; locus:2059899; AT2G16730.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q9SCU9; -.
DR OMA; HWTRKND; -.
DR OrthoDB; 179316at2759; -.
DR PhylomeDB; Q9SCU9; -.
DR BioCyc; ARA:AT2G16730-MON; -.
DR PRO; PR:Q9SCU9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SCU9; baseline and differential.
DR Genevisible; Q9SCU9; 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 Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..848
FT /note="Beta-galactosidase 13"
FT /id="PRO_5000065886"
FT DOMAIN 754..843
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 271
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 848 AA; 95900 MW; 1AF1AF48C1FA5F1B CRC64;
MKIHSSDHSW LLLAVLVILL SFSGALSSDD KEKKTKSVDK KKEVTYDGTS LIINGNRELL
YSGSIHYPRS TPEMWPNIIK RAKQGGLNTI QTYVFWNVHE PEQGKFNFSG RADLVKFIKL
IEKNGLYVTL RLGPFIQAEW THGGLPYWLR EVPGIFFRTD NEPFKEHTER YVKVVLDMMK
EEKLFASQGG PIILGQIENE YSAVQRAYKE DGLNYIKWAS KLVHSMDLGI PWVMCKQNDA
PDPMINACNG RHCGDTFPGP NKDNKPSLWT ENWTTQFRVF GDPPAQRSVE DIAYSVARFF
SKNGTHVNYY MYHGGTNFGR TSAHYVTTRY YDDAPLDEFG LEREPKYGHL KHLHNALNLC
KKALLWGQPR VEKPSNETEI RYYEQPGTKV CAAFLANNNT EAAEKIKFRG KEYLIPHRSI
SILPDCKTVV YNTGEIISHH TSRNFMKSKK ANKNFDFKVF TESVPSKIKG DSFIPVELYG
LTKDESDYGW YTTSFKIDDN DLSKKKGGKP NLRIASLGHA LHVWLNGEYL GNGHGSHEEK
SFVFQKPVTL KEGENHLTML GVLTGFPDSG SYMEHRYTGP RSVSILGLGS GTLDLTEENK
WGNKVGMEGE RLGIHAEEGL KKVKWEKASG KEPGMTWYQT YFDAPESQSA AAIRMNGMGK
GLIWVNGEGV GRYWMSFLSP LGQPTQIEYH IPRSFLKPKK NLLVIFEEEP NVKPELIDFV
IVNRDTVCSY IGENYTPSVR HWTRKNDQVQ AITDDVHLTA NLKCSGTKKI SAVEFASFGN
PNGTCGNFTL GSCNAPVSKK VVEKYCLGKA ECVIPVNKST FEQDKKDSCP KVEKKLAVQV
KCGRDKKN
