ID   BGA15_ARATH             Reviewed;         779 AA.
AC   Q9C6W4; F4IAX4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Beta-galactosidase 15;
DE            Short=Lactase 15;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   Name=BGAL15; OrderedLocusNames=At1g31740; ORFNames=F27M3.5;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
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   [3]
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   [4]
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 levels in roots and
CC       siliques. {ECO:0000269|PubMed:16267099}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; AC074360; AAG60136.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31387.2; -; Genomic_DNA.
DR   RefSeq; NP_001319124.1; NM_001332978.1.
DR   AlphaFoldDB; Q9C6W4; -.
DR   SMR; Q9C6W4; -.
DR   STRING; 3702.Q9C6W4; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; Q9C6W4; 7 sites, No reported glycans.
DR   PaxDb; 3702-AT1G31740-1; -.
DR   ProteomicsDB; 240857; -.
DR   EnsemblPlants; AT1G31740.1; AT1G31740.1; AT1G31740.
DR   GeneID; 840061; -.
DR   Gramene; AT1G31740.1; AT1G31740.1; AT1G31740.
DR   KEGG; ath:AT1G31740; -.
DR   Araport; AT1G31740; -.
DR   TAIR; AT1G31740; BGAL15.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   InParanoid; Q9C6W4; -.
DR   OMA; TYNTAKI; -.
DR   OrthoDB; 5489808at2759; -.
DR   PhylomeDB; Q9C6W4; -.
DR   BioCyc; ARA:AT1G31740-MONOMER; -.
DR   PRO; PR:Q9C6W4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C6W4; baseline and differential.
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   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; BETA-GALACTOSIDASE RELATED; 1.
DR   PANTHER; PTHR23421:SF137; BETA-GALACTOSIDASE-RELATED; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 2.
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   Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..779
FT                   /note="Beta-galactosidase 15"
FT                   /id="PRO_0000293094"
FT   DOMAIN          694..779
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   ACT_SITE        178
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        247
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        555
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   779 AA;  86342 MW;  888813DF318890B0 CRC64;
     MVSLSFILCC VLVSSCAYAT IVSHDGRAIT IDGHRRVLLS GSIHYPRSTT EMWPDLIKKG
     KEGSLDAIET YVFWNAHEPT RRQYDFSGNL DLIRFLKTIQ NEGMYGVLRI GPYVCAEWNY
     GGFPVWLHNM PGMEFRTTNT AFMNEMQNFT TMIVEMVKKE KLFASQGGPI ILAQIENEYG
     NVIGSYGEAG KAYIQWCANM ANSLDVGVPW IMCQQDDAPQ PMLNTCNGYY CDNFSPNNPN
     TPKMWTENWT GWYKNWGGKD PHRTTEDVAF AVARFFQKEG TFQNYYMYHG GTNFDRTAGG
     PYITTTYDYD APLDEFGNLN QPKYGHLKQL HDVLHAMEKT LTYGNISTVD FGNLVTATVY
     QTEEGSSCFI GNVNETSDAK INFQGTSYDV PAWSVSILPD CKTETYNTAK INTQTSVMVK
     KANEAENEPS TLKWSWRPEN IDSVLLKGKG ESTMRQLFDQ KVVSNDESDY LWYMTTVNLK
     EQDPVLGKNM SLRINSTAHV LHAFVNGQHI GNYRVENGKF HYVFEQDAKF NPGANVITLL
     SITVGLPNYG AFFENFSAGI TGPVFIIGRN GDETIVKDLS THKWSYKTGL SGFENQLFSS
     ESPSTWSAPL GSEPVVVDLL GLGKGTAWIN GNNIGRYWPA FLSDIDGCSA EYHVPRSFLN
     SEGDNTLVLF EEIGGNPSLV NFQTIGVGSV CANVYEKNVL ELSCNGKPIS AIKFASFGNP
     GGDCGSFEKG TCEASNNAAA ILTQECVGKE KCSIDVSEDK FGAAECGALA KRLAVEAIC
//