ID H9D2I1_MOMCH Unreviewed; 719 AA.
AC H9D2I1;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
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};
OS Momordica charantia (Bitter gourd) (Balsam pear).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Momordiceae; Momordica.
OX NCBI_TaxID=3673 {ECO:0000313|EMBL:AFD54987.1};
RN [1] {ECO:0000313|EMBL:AFD54987.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Fruit {ECO:0000313|EMBL:AFD54987.1};
RA Gao S., Li Y.Z., Pan D.M., Chen G.X., Chen Y.Z.;
RT "Cloning and expressing analysis of beta-galactosidase gene in bitter
RT gourd.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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; JQ581596; AFD54987.1; -; mRNA.
DR AlphaFoldDB; H9D2I1; -.
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; 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 PANTHER; PTHR23421:SF63; BETA-GALACTOSIDASE 12; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 2.
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 2: Evidence at transcript level;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..719
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003618585"
FT DOMAIN 29..332
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 355..411
FT /note="Beta-galactosidase beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF17834"
FT DOMAIN 462..529
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT DOMAIN 611..697
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
SQ SEQUENCE 719 AA; 80354 MW; 439F01BA480CE2A1 CRC64;
MSKCVLLFLG LLSWVCYAMA TVTYDQKAII INGKRRILVS GSIHYPRSTP QMWPSLIQNA
KDGGLDIIET YVFWNGHEPT QGKYYFEDRY DLVRFIKLVQ QAGLYVHLRI GPYVCAEWNY
GGFPIWLKHV PGIVFRTENE PFKAAMQKFT EKIVGMMKSE KLYESQGGPI ILSQIENEYG
PVEWEIGAPG KSYTKWAAQM ALGLDTGVPW VMCKQEDAPD PVIDTCNGFY CENFKPNREN
KPKIWTEVWS GWYTAFGGAV PYRPAEDLAF SVARFVQNGG SLFNYYMYHG GTNFGRSSGL
FIANSYDFDA PIDEYGLKRE PKWEHLRDLH KAIKLCEPAL VSADPNVTWL GKNLEARVFK
SSSGACAAFL ANYDISTSSK VSFWNTQYDL PPWSISILSD CKSAIFNTAR IGAQSAPMKM
MLVSSFWWLS YKEEVASGYA TDTTTKDGLV EQVNFTWDST DYLWYMTDIQ IDPNEAFIKS
GQWPLLNISS AGHVLHVFVN GQLSGTVYGS LENPKVAFSK YVNLKAGVNK LSMLSVTVGL
PNVGLHFESW NAGVLGPVTL KGLNEGIRDM SGYKWSHKVG LKGENMNLHT IGGSNSVQWA
KGSGLVQKQP LTWYKTNFNT PAGNEPLALD MSSMGKGQIW INGRSIGRYW PAYAASGSCG
KCSYAGIFTE KKCLSNCGQP SQKWYHVPRE WLESKGNFLV VFEELGGNPG GISLVKRSP
//