ID A0A3B6RIR4_WHEAT Unreviewed; 839 AA.
AC A0A3B6RIR4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 ORFNames=CFC21_097750 {ECO:0000313|EMBL:KAF7095633.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS7A02G272400.3};
RN [1] {ECO:0000313|EMBL:KAF7095633.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7095633.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS7A02G272400.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS7A02G272400.3};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS7A02G272400.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7095633.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7095633.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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; CM022229; KAF7095633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6RIR4; -.
DR EnsemblPlants; TraesCS7A02G272400.3; TraesCS7A02G272400.3; TraesCS7A02G272400.
DR Gramene; TraesCS7A02G272400.3; TraesCS7A02G272400.3; TraesCS7A02G272400.
DR Gramene; TraesCS7A03G0635900.3; TraesCS7A03G0635900.3.CDS; TraesCS7A03G0635900.
DR Gramene; TraesKAR7A01G0186400.2; cds.TraesKAR7A01G0186400.2; TraesKAR7A01G0186400.
DR Proteomes; UP000019116; Chromosome 7A.
DR Proteomes; UP000815260; Chromosome 7A.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
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; 1.
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:SF52; BETA-GALACTOSIDASE 14; 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.
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:UP000019116};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..839
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039994779"
FT DOMAIN 744..831
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 839 AA; 94556 MW; E27E7484F9824E7D CRC64;
MSLLHVRLAA AAIAVVALVA GGDAYQLTKP GTVISYDRRS LMVDGQRDIF FSGSIHYPRS
PFHEWPDLIA RAKEGGLNVI ESYVFWNVHE PEMGVYNFEG RYDMIKFFKL IQEHEMYAMV
RIGPFVQAEW NHGGLPYWLR EVPDIIFRTD NEPFKKLMQK FVTLVVNKLK EAKLFASQGG
PIILAQIENE YQHMEAAFKE NGTRYIEWAA KMAISTDIGV PWIMCKQTKA PADVIPTCNG
RHCGDTWPGP VDKNKPLLWT ENWTAQYRVF GDPPSQRSAE DIAFAVARFF SVGGSMVNYY
MYHGGTNFGR TGASFVMPRY YDEAPLDEFG MFKEPKWGHL KDLHHALRLC KNALLFGTPS
TQPLGKLYEA RVFEIPEQKV CVAFLSNHNT KEDGTVTFRG QKYFVPRRSV SILGDCKTVV
FSTQYVNAQH NQRTFHFTDQ TVQNNVWEMY TEGDQVPTYK FSTDRSEKPL EAYNMTKDKT
DYLWYTTSFL LDPEDLPSRL DIKPVLEASS HGHAMVAFVN KKLVGCGHGT KMNKAFSLEK
PIDVKVGINH ISILSSTLGL QDSGSYLERR QAGVHSVTIQ GLNTGTLDLT SNGWGHIVGL
DGERKQAFTE KGGEVQWQPA VFDKPLTWYR RRFDMPSGED PVVIDMNPMG KGILFVNGEG
LGRYWSSYKH ALGRPSQYLY HVPRCFLKPT GNVLTIFEEE GGRPDAIMIL TVKRDNICSF
ISETNPGHVR SWETKDSQLT MVADDLKPRA VLTCPEKKMI QQVVFASYGN PLGICGNYTF
GNCHTPKAKE IVEKACVGKR SCVLAVSHEV YGGDLNCPGT TATLAVQAKC SKRQRTAEQ
//
