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Database: UniProt
Entry: A0A1S3BQ79_CUCME
LinkDB: A0A1S3BQ79_CUCME
Original site: A0A1S3BQ79_CUCME 
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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