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   24-JAN-2024, entry version 146.
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.Q9SCU9; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; Q9SCU9; 8 sites, No reported glycans.
DR   PaxDb; 3702-AT2G16730-1; -.
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; AT2G16730; BGAL13.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   InParanoid; Q9SCU9; -.
DR   OMA; PEMWPNI; -.
DR   OrthoDB; 1204541at2759; -.
DR   PhylomeDB; Q9SCU9; -.
DR   BioCyc; ARA:AT2G16730-MONOMER; -.
DR   PRO; PR:Q9SCU9; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SCU9; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; TAS:TAIR.
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:SF176; BETA-GALACTOSIDASE 13; 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; Q9SCU9; AT.
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
//