ID A0A444WUS2_ARAHY Unreviewed; 829 AA.
AC A0A444WUS2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=Ahy_Scaffold1g107127 {ECO:0000313|EMBL:RYQ81122.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ81122.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ81122.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYQ81122.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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}.
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:RYQ81122.1}.
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DR EMBL; SDMP01000021; RYQ81122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444WUS2; -.
DR STRING; 3818.A0A444WUS2; -.
DR OrthoDB; 1204541at2759; -.
DR Proteomes; UP000289738; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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; 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 InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR PANTHER; PTHR23421:SF52; BETA-GALACTOSIDASE 14; 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:UP000289738};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..829
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019343043"
FT DOMAIN 738..826
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 829 AA; 93015 MW; BE7A625A27DE347D CRC64;
MMLTITSRGL FLTALVTQLF VSVVSNGPAK GVTYDGKSLF INGRRMLLFS GSIHYPRCPP
EMWPNIFKKA KEGGLNVIQT YVFWNIHEPV QGQFNFEGDY DLVKYIKTIG ENGMYATLRV
GPFIEAEWNY GGLPVWLKHV PNITFRSDNE PFMYHMEKFT KMIIKKMMDE KLFASQGGPI
ILSQIENEYN TVQKAYKEHG TAYVHWAGDM AVGLNTGVPW IMCKQSDAPG SVINTCNGRN
CGDTFVGPNS PNKPILWTEN WTAQYRAFGD PPSQRTAEDI AFSIARFFSK NGTLANYYMY
YGGTNFGRTT SSFITTRYYD EAPLDEYGLQ REPKWGHLRN LHDALKLSQK ALLWGTPSLQ
EFSDDTEARV YEGKGNTCTA FLSNNNTLLD ATVEFRGVKY YLPPRSISIL PDCKIVVYNS
RMIVSQHNER RYKDSNIANN LQWTMFKETI PTPDTSPLKF VEPLEHFSTT KDDSDYLWFT
TSLKLDATQL NSATGRLVLE ITSLGHLLHA FVNGEYIGSG HGTLIRKNFV FKKPISLKPG
INYISILGAT VGFPDSGSYL EHRVAGVRAI TLLGLKTSPL DLSRKGWSHK ISLDGEKNNI
FTEQGSQKVK WTKADKGAAL TWYKANFDAP EGNDPVAIQM ETMSKGMVWV NGKSIGRYWP
SYLSPLGNPS QGIYHIPRAF LKPKENLIVV LEEMGGKVEG IKIQTVNRDT ICSIVREDYP
PNAKTWRREM GVVSTKMKNP KPTANLACPE NKIITHVEFA SYGDPVGECG HLFPGNCTSP
NSQKVVEQYC LGKAKCAVPL DKNIFDKQGK LCPNNLKTLA VQAHCGHQT
//
