ID I1HNC6_BRADI Unreviewed; 829 AA.
AC I1HNC6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=100839503 {ECO:0000313|EnsemblPlants:PNT72151};
GN ORFNames=BRADI_2g40450v3 {ECO:0000313|EMBL:PNT72151.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:PNT72151.1};
RN [1] {ECO:0000313|EMBL:PNT72151.1, ECO:0000313|EnsemblPlants:PNT72151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT72151.1,
RC ECO:0000313|EnsemblPlants:PNT72151};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:PNT72151.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT72151.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:PNT72151}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:PNT72151};
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}.
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DR EMBL; CM000881; PNT72151.1; -; Genomic_DNA.
DR RefSeq; XP_003566745.1; XM_003566697.2.
DR AlphaFoldDB; I1HNC6; -.
DR EnsemblPlants; PNT72151; PNT72151; BRADI_2g40450v3.
DR GeneID; 100839503; -.
DR Gramene; PNT72151; PNT72151; BRADI_2g40450v3.
DR KEGG; bdi:100839503; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; I1HNC6; -.
DR OMA; TYNTAKI; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000008810; Chromosome 2.
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; IPR025300; BetaGal_jelly_roll_dom.
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:SF174; BETA-GALACTOSIDASE 7; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000008810};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..829
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003643704"
FT DOMAIN 746..829
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 829 AA; 91787 MW; 8750AE734321BAE8 CRC64;
MATTTMARAS LALVLLLITA AVGAANCTTV AYNDRALVID GQRRIVLSGS IHYPRSTPEM
WPDLIKKAKE GGLDAIETYV FWNGHEPRPR QYNFAGNYDI VRFFKEIQNA GMYAILRIGP
YICGEWNYGG LPAWLRDIPG MQFRMHNQPF EHEMETFTTL IVNKLKDANM FAGQGGPIIL
SQIENEYGNI MANLTDAQSA SEYIHWCAAM ANKQNVGVPW IMCQQDADVP PNVINTCNGF
YCHDWFPKRT DIPKIWTENW TGWFKAWDKP DFHRSAQDIA FAVAMFFQKR GSLQNYYMYH
GGTNFGRTAG GPYITTSYDY DAPLDEYGNI REPKYGHLKD LHAVLKSMEK ILVHGDFSDI
NYGRNVTVTK YTLDGSSVCF ISNQFDDRDA NATIDGTTHV VPAWSVSVLP DCKAVAYNTA
KIKAQTSVMV KKPNTVEQEP ENLKWSWMPE HLKPFMTDEK GSFRKNELLE QITTSTDQSD
YLWYRTSFEH KGEAKYKLSV NTTGHQIYAF VNGKLAGRQH SPNGAFIFQL ESPVKLHDGK
NYLSLLSATM GLKNYGALFE LMPAGIVGGP VKLVDNNGST IDLSNSSWSY KAGLAGEHRQ
IHLDKPGYKW HGDNGTIPIN RAFTWYKATF QAPAGEEAVV ADLMGLNKGV AWVNGNNLGR
YWPSYVAAEM GGCHHCDYRG AFKAEGDGLK CLTGCNEPAQ RFYHVPRVFL RAGEPNTVVL
FEEAGGDPSR VGFHTVAVGP VCVEAAEKGD NVTLSCGQHK GRTISSVDLA SYGVTRGQCG
AYQGGCESKA AYEAFAEACV GKESCTVQHT DAFSGAGCQS GVLTVQATC
//
