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}.
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; 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
//