ID K3XEK0_SETIT Unreviewed; 825 AA.
AC K3XEK0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 65.
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};
GN Name=101765698 {ECO:0000313|EnsemblPlants:KQL06258};
GN ORFNames=SETIT_5G258600v2 {ECO:0000313|EMBL:RCV26597.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV26597.1};
RN [1] {ECO:0000313|EMBL:RCV26597.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL06258,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV26597.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV26597.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV26597.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQL06258}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL06258};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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}.
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; AGNK02003236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003532; RCV26597.1; -; Genomic_DNA.
DR RefSeq; XP_004969419.1; XM_004969362.3.
DR AlphaFoldDB; K3XEK0; -.
DR EnsemblPlants; KQL06258; KQL06258; SETIT_000317mg.
DR GeneID; 101765698; -.
DR Gramene; KQL06258; KQL06258; SETIT_000317mg.
DR KEGG; sita:101765698; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; K3XEK0; -.
DR OMA; SYEMQAS; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000004995; Chromosome V.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..825
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010125636"
FT DOMAIN 739..825
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 825 AA; 91582 MW; 527ACF9DFA4FB8C1 CRC64;
MAPPAFAYAA VAVAVLAAAA SAAVTYDRKA VVVNGQRRIL LSGSIHYPRS VPEMWPDLIQ
KAKDGGLDVV QTYVFWNGHE PSPGQYYFEG RYDLVHFIKL VKQAGLYVHL RIGPYVCAEW
NFGGFPVWLK YVPGIRFRTD NEPFKSEMQK FTTKIVDMMK SEGLFEWQGG PIILSQIENE
FGPLEWDQGE PAKAYASWAA NMAVALNTGV PWIMCKEDDA PDPIINTCNG FYCDWFSPNK
PHKPTMWTEA WTAWYTGFGI PVPHRPVEDL AYGVAKFIQK GGSFVNYYMY HGGTNFGRTA
GGPFIATSYD YDAPIDEYGL LREPKWGHLK ELHKAIKLCE PALVAGDPIV TSLGNAQQAS
VFRSSTGACV AFLENKDKVS YARVAFNGMH YGLPPWSISI LPDCKTTVYN TARVGSQISQ
MKMEWAGGLT WQSYNEDINS LGEESFTTIG LLEQINVTRD KTDYLWYTTY VEIAQDEQFL
SNGKNPTLTV MSAGHALHIF INGQLTGTVY GNVEDPRLTY RGSVKLWPGS NTVSCLSIAV
GLPNVGEHFE TWNAGILGPV TLDGLNEGRR DLTWQKWTYQ VGLKGETLSL HSLSGSSSVE
WGEPVQKQPL TWYKAFFNAP DGDEPLALDM SSMGKGQIWI NGQGIGRYWP GYKASGTCGN
CDYRGEYDEK KCQTNCGDSS QRWYHVPRSW LNPTGNLLVI FEEWGGDPTG ISMVKRTTGS
ICADVSEWQP SMKSWHTKDY EKAKVHLQCD HGRKITEIKF ASFGTPQGSC GSYSEGTCHA
HKSYDIFLKN CIGQERCGVS VVPDVFGGDP CPGTMKRAVV EAICG
//
