ID I1HTW7_BRADI Unreviewed; 846 AA.
AC I1HTW7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=BRADI_2g56607v3 {ECO:0000313|EMBL:KQK10850.1};
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|EnsemblPlants:KQK10850};
RN [1] {ECO:0000313|EMBL:KQK10850.1, ECO:0000313|EnsemblPlants:KQK10850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK10850.1,
RC ECO:0000313|EnsemblPlants:KQK10850};
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:KQK10850.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK10850.1};
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:KQK10850}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK10850};
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 -!- 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; KQK10850.1; -; Genomic_DNA.
DR AlphaFoldDB; I1HTW7; -.
DR STRING; 15368.I1HTW7; -.
DR EnsemblPlants; KQK10850; KQK10850; BRADI_2g56607v3.
DR Gramene; KQK10850; KQK10850; BRADI_2g56607v3.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; I1HTW7; -.
DR OMA; NGTHSPF; -.
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; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR041392; GHD.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
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:SF67; BETA-GALACTOSIDASE 10; 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; PS50228; SUEL_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..846
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014094852"
FT DOMAIN 760..846
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 846 AA; 94103 MW; A61A0DE5EC3DBA8A CRC64;
MAAAPVRFLP LLLPLLLPLL LLLVAAAADS GVTYDGRSLI ISGRRRLLIS TSIHYPRSVP
AMWPKLVAEA KDGGADCIET YVFWNGHETA PGEYYFEDRF DLVRFAKVVK DAGLYLMLRI
GPFVAAEWNF GGVPVWLHYI PGAVFRTNNE PFKSHMKSFT TKIVDMMKRE RFFASQGGHI
ILAQIENEYG DTEQAYGADG KAYAMWAASM ALAQNTGVPW IMCQQYDAPE HVINTCNSFY
CDQFKTNSPT KPKIWTENWP GWFQTFGESN PHRPPEDVAF SVARFFQKGG SVQNYYVYHG
GTNFGRTTGG PFITTSYDYD APIDEYGLTR LPKWAHLRDL HKSIKLCEHS LLYGNLTSLS
LGTKQEADVY TDHSGGCVAF LANIDPENDT VVTFRSRQYD LPAWSVSILP DCKNAVFNTA
KVQSQTLMVD MVPETLQSTK PDRWSIFREK TGIWDKNDFI RNGFVDHINT TKDSTDYLWH
TTSFNVDRSY PTNGNRELLS IDSKGHAVHA FLNNELIGSA YGNGSKSSFN VHMPIKLKPG
KNEIALLSMT VGLQNAGPHY EWVGAGLTSV NISGMKNGSI DLSSNNWAYK IGLEGEHYGL
FKPDQGNNQR WSPQSEPPKG QPLTWYKVNV DVPQGDDPVG IDMQSMGKGL AWLNGNAIGR
YWPRTSSSDD RCTPSCNYRG PFNPSKCRTG CGKPTQRWYH VPRSWFHPSG NTLVVFEEQG
GDPTKITFSR RVATKVCSFV SENYPSIDLE SWDKSISDDG KDTAKVQLSC PKGKNISSVK
FASFGDPSGT CRSYQQGRCH HPSSLSVVEK ACLNINSCTV SLSDEGFGKD LCPGVAKTLA
IEADCS
//
