ID A0A453EYX1_AEGTS Unreviewed; 938 AA.
AC A0A453EYX1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET3Gv20516900.2, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET3Gv20516900.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU000675};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000256|ARBA:ARBA00004271}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR AlphaFoldDB; A0A453EYX1; -.
DR EnsemblPlants; AET3Gv20516900.2; AET3Gv20516900.2; AET3Gv20516900.
DR Gramene; AET3Gv20516900.2; AET3Gv20516900.2; AET3Gv20516900.
DR OMA; SPSVEWV; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000015105; Chromosome 3D.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF153; BETA-GALACTOSIDASE 2; 1.
DR PANTHER; PTHR23421; 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 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 114..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 852..938
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 104413 MW; D9B9F1E3B59E53FB CRC64;
MNASHAGSFK KERGNEAQNY RRCRSGVPEG KQEKGKGNQL QTLDGEGRVN LTKPKRVCPP
ASASLRFTSL RSHSRWREKH RKAPRFRFFF SPHFPPFPAS VLPMASSALP APSVVAVAVA
VAFAVATLAA TASAAVTYDR KALVVNGRRR ILLSGSIHYP RSVPDMWPDL IQKAKDGGLD
VVQTYVFWNG HEPSPGQYYF EGRYDLVRFI KLVKQAGLYV HLRIGPYVCA EWNFGGFPVW
LKYVPGISFR TDNQPFKLEM QKFTTKIVDM MKSEGLFEWQ GGPIILSQIE NEFGPLEWDQ
GEPSKAYASW AANMAIALDT GVPWIMCKED DAPDPIINTC NGFYCDWFSP NKPHKPTMWT
EAWTAWYTGF GVPVPHRPVE DLAYGVAKFI QKGGSFVNYY MYHGGTNFGR TAGGPFVATS
YDYDAPIDEY GLLREPKWGH LKELHRAIKL CEPALVAGDP IISSLGKAQK SSVFRSSTGA
CAAFLENKDK LSYARVSFSG MHYDLPPWSI SILPDCKTTV FNTARVGSQI SQMKMEWAGG
LTWQSYNEEI NSYSEEEAFT AVGLLEQINM TRDNTDYLWY TTYVDVAKDE QFLTSGKSPK
LTVMSAGHAL HVFVNGQLTG TVYGSVEDPK LTYTGSVKLW AGSNTISCLS IAVGLPNVGE
HFETWNAGIL GPVILYGLNE GRRDLTWQKW TYQVGLKGEA MSLHSLSGSS SVEWGEPVQK
QPLTWYKAFF NAPDGDEPLA LDMNSMGKGQ IWINGQGIGR YWPGYKAPGT CGYCDYRGEY
NETKCQTNCG DSSQRWYHVP RPWLNPTGNL LVIFEEIGGD PSEISMVKRT TGSVCADVSE
WQPSMTNWRT KDYEKAKVHL QCDHGRKITE IKFASFGTPQ GSCGSYSEGG CHAHKSYDIF
RKNCINQEHC AVCVVPEVFG GDPCPGTMKR AVVEVMCG
//
