ID A0A1S3BQ79_CUCME Unreviewed; 721 AA.
AC A0A1S3BQ79;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 Name=LOC103492322 {ECO:0000313|RefSeq:XP_008450853.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008450853.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|RefSeq:XP_008450853.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_008450853.1; XM_008452631.2.
DR AlphaFoldDB; A0A1S3BQ79; -.
DR GeneID; 103492322; -.
DR KEGG; cmo:103492322; -.
DR eggNOG; KOG0496; Eukaryota.
DR InParanoid; A0A1S3BQ79; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000089565; Unplaced.
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 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:UP000089565};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..721
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010175191"
FT DOMAIN 29..333
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 356..412
FT /note="Beta-galactosidase beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF17834"
FT DOMAIN 463..530
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT DOMAIN 612..698
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
SQ SEQUENCE 721 AA; 80167 MW; 95AC075456C9E76B CRC64;
MLKMSKIMVV FLWVCSSVMA SVTYDHKAII INGRRRILIS GSIHYPRSTP QMWPDLIQKA
KDGGLDVIDT YVFWNGHEPS PGHYNFEDRY DLVRFVKLVQ QAGLYVHLRI GPYVCAEWNF
GGFPVWLKYV PGIAFRTDNG PFKAAMQKFT EKIVGVMKGE KLYESQGGPI ILSQIENEYG
PVEWEIGAPG KSYSKWAAQM ALDLDTGVPW VMCKQDDAPD PVIDTCNGFY CENFKPNQVY
KPKMWTEAWT GWFTEFGGPA PYRPVEDMAY SVARFIQNGG SFINYYMYHG GTNFGRTAGG
PFIATSYDYD APIDEYGLLR EPKWSHLRDL HKAIKLCEPA LVSVDPTVSS LGSNQEAHVF
KTRSGSCAAF LANYDASSSA TVTFGNNQYD LPPWSVSILP DCKSAVFNTA KVGAPTSQPK
MTPVSSFSWL SYNEETASAY TEDTTTMAGL VEQISVTRDS TDYLWYMTDI RIDPNEGFLK
SGQWPLLTVF SAGHALHVFI NGQLSGTTYG GAENYKLTFS KYVNLRAGIN KLSILSVAVG
LPNGGLHYET WNTGILGPVT LKGLNEDTRD MSGYKWSYKI GLKGEALNLH TASGSSSVEW
VAGSLVAQKQ PLTWYKTTFD SPEGNEPLAL DMSSMGKGQI WINGQSIGRH WPAYTARGSC
GKCNYGGIFN EKKCHSNCGE PSQRWYHIPR AWLKSSGNML VIFEEWGGNP EGISLVKRSI
S
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