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Database: UniProt
Entry: A0A2P6RSY7_ROSCH
LinkDB: A0A2P6RSY7_ROSCH
Original site: A0A2P6RSY7_ROSCH 
ID   A0A2P6RSY7_ROSCH        Unreviewed;       735 AA.
AC   A0A2P6RSY7;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=RchiOBHm_Chr2g0122851 {ECO:0000313|EMBL:PRQ49521.1};
OS   Rosa chinensis (China rose).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC   Rosa.
OX   NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ49521.1, ECO:0000313|Proteomes:UP000238479};
RN   [1] {ECO:0000313|EMBL:PRQ49521.1, ECO:0000313|Proteomes:UP000238479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA   Bendahmane M.;
RT   "The Rosa genome provides new insights in the design of modern roses.";
RL   Nat. Genet. 0:0-0(2018).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PRQ49521.1}.
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DR   EMBL; PDCK01000040; PRQ49521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P6RSY7; -.
DR   EnsemblPlants; PRQ49521; PRQ49521; RchiOBHm_Chr2g0122851.
DR   Gramene; PRQ49521; PRQ49521; RchiOBHm_Chr2g0122851.
DR   OMA; WIMCKSP; -.
DR   Proteomes; UP000238479; Chromosome 2.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   PANTHER; PTHR23421:SF179; BETA-GALACTOSIDASE 6; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 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.
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:UP000238479};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..735
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015108687"
FT   DOMAIN          35..352
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          375..432
FT                   /note="Beta-galactosidase beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF17834"
FT   DOMAIN          629..695
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
SQ   SEQUENCE   735 AA;  83312 MW;  A300BBD58A54B057 CRC64;
     MEWRWLQFWV MVVVVLITDE RVSVSGGNVT YDGRSLIIDG QRKILFSGSI HYPRSTPEMW
     PSLIGKAKEG GLDVIQTYVF WNLHEPQPGQ YDFSGRYDLV KFIKEIQAQG LYACLRIGPF
     IESEWTYGGF PFWLHDVPGI VYRTDNEPFK ACTLPITNYI FYMQNFTTKI VNLMKSEGLY
     ASQGGPIILS QIENEYQNVE AAFHEKGPAY VRWAAKMAVD LQTGVPWVMC KQTDAPDPVI
     NTCNGMQCGK TFGGPNSPNK PSMWTENWTS FYQVYGGEPY IRSAENIAFH VALFIARLNG
     SYVNYYMYHG GTNFGRTSSA YVITGYYDQA PLDEYGLLRQ PKWGHLKQLH AAFRNCSTTL
     LQGMRTNFSL GQLQEAYVFQ EESAGRCVAF LVNNDEKTNA TVQFRNISYD LMPMSISILP
     DCENVIFNTA KVNTSSNKRI TRSAQIFDSV DSWEGSKDVI QNFEPTISLQ SDTLLEHMNV
     TKDKSDYLWY TMRFQHNISC TEPVLRVESF GHVTHAFVNG INTGNAHGSH DTKQFIMEIP
     VLLNDGSNNI SLLSVMVGLP DSGAFLESKF AGLKRVEIHC NETDQFYNFT NYAWGYQVGL
     LGEKLQIYRE ENLDNIEWNN IEGYFNQSLT WYMTFFDAPV GNDPVGLNLS SMAKGEAWIN
     GQSIGRYWVS FLTSKGQPSQ SMYHVPRSFL KDSENLLVLL EEVGGNPLHI SLDTISLSSL
     SESTSYHQIP SISLE
//
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