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Database: UniProt
Entry: A0A022PX73_ERYGU
LinkDB: A0A022PX73_ERYGU
Original site: A0A022PX73_ERYGU 
ID   A0A022PX73_ERYGU        Unreviewed;       848 AA.
AC   A0A022PX73;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=MIMGU_mgv1a001274mg {ECO:0000313|EMBL:EYU18850.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU18850.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU18850.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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}.
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DR   EMBL; KI632313; EYU18850.1; -; Genomic_DNA.
DR   RefSeq; XP_012827836.1; XM_012972382.1.
DR   AlphaFoldDB; A0A022PX73; -.
DR   STRING; 4155.A0A022PX73; -.
DR   GeneID; 105949108; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   OrthoDB; 5489808at2759; -.
DR   PhylomeDB; A0A022PX73; -.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
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:SF124; BETA-GALACTOSIDASE 2-RELATED; 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:UP000030748};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..848
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001506373"
FT   DOMAIN          761..848
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   848 AA;  93058 MW;  655E1072683BECC3 CRC64;
     MAGSRAAAVV FLLLAASASL CTAVSVDYDG RALVIDGKRR VLVSGSIHYP RSTPDMWPDL
     IKKSKEGGLD IIETYVFWDM HEPVRGQYDF TERKDLVKFV KLVAEAGLYL HLRIGPYVCA
     EWNYGGFPLW LHFLPGIQLR TDNDVYKAEM QRFTAKIVGM MKQNNLYASQ GGPIVLSQIE
     NEYGNIDWQY GSSAKPYIDW AAQMATSMNT GVPWVMCQQN NAPDPMINTC NGFYCDQFTP
     NSPSKPKFWT ELWSGWFSAW GNPVPYRPVE DVAFAAARFY QNNGTLLNYY MYHGGTNFAR
     TSGGPFITTS YDYDSPIDEY GLLRQPKWGH LKDLHKAIKL CEEAMVSTVG NTTSLGQNLE
     VTVYRAESGE CAAFLANFDW QLDATVTFNG NSYDLPAWSV SILPDCKNVV YNTAKVNAIT
     ALTKFVPQTS QSGSNSSVVS LSSWSWFKEP VGISLNKEAF VLPGLVEQIN TTADKSDFLW
     YSLSIDLNAN DPLLKEGSQI LLHLDSVGHG LYAFVNGDLA GSGKGSSSNN KFSMDVPMNL
     EPGNNTIDLL CLTVGLSNYG AFFDTYTAGI GGPVQFKGLA NGSTIDLSSQ QWTYQVGLKG
     EQLGLSNGVS GQWDSQPALP KNTPLTWYKT TFSAPAGNSP VAIDFTGMGK GHAWVNGHGI
     GRYWPANVAP SNGNCADTCN YRGSYSNNKC LKGCGKPTQQ QYHVPRSWLK PTGNTLVVLE
     EIGGDPTMIS FATRELGLIC GKVSENYPAP LDLWDSNYLT RVTKPTLLLE CPSPSQVIKR
     LQFVSFGNPH GGCGGYTHGR CRSKRARRVI HRACTGKTKC SIDVTVENLG DPNCENVTKS
     LAVEAFCG
//
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