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Database: UniProt
Entry: A0A1D6MYX9_MAIZE
LinkDB: A0A1D6MYX9_MAIZE
Original site: A0A1D6MYX9_MAIZE 
ID   A0A1D6MYX9_MAIZE        Unreviewed;       841 AA.
AC   A0A1D6MYX9;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=ZEAMMB73_Zm00001d041880 {ECO:0000313|EMBL:ONM33893.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM33893.1};
RN   [1] {ECO:0000313|EMBL:ONM33893.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM33893.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) 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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000256|ARBA:ARBA00004271}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; CM007649; ONM33893.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6MYX9; -.
DR   ExpressionAtlas; A0A1D6MYX9; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
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; 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:SF13; BETA-GALACTOSIDASE 9; 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}.
SQ   SEQUENCE   841 AA;  93686 MW;  7FC9C9FCB4358D03 CRC64;
     MLVSAGLHYP RATPEMWPSL IAKCKEGGVD AIETYVFWNG HEPAKGQYYF EGRFDIVRFA
     KLVAAEGLFL FLRIGPYACA EWNFGGFPVW LRDVPGIEFR TDNEPYKAEM QIFVTKIVDI
     MKEEKLYSWQ GGPIILQQIE NEYGNIQGHY GQAGKRYMLW AAQMALALDT GVPWVMCRQT
     DAPEQILNTC NAFYCDGFKP NSYNKPTIWT EDWDGWYADW GESLPHRPAQ DSAFAVARFY
     QRGGSLQNYY MYFGGTNFER TAGGPLQITS YDYDAPIDEY GILRQPKWGH LKDLHAAIKL
     CESALTAVDG SPHYVKLGPM QEAHVYSSEN VHTNGSISGN SQFCSAFLAN IDEHKYASVW
     IFGKSYSLPP WSVSILPDCE TVAFNTARVG TQTSFFNVES GSPSYSSRHK PRILSLIGVP
     YLSTTWWTFK EPVGIWGEGI FTAQGILEHL NVTKDISDYL SYTTRVNISE EDVLYWNSKG
     FLPSLTIDQI RDVARVFVNG KLAGSKVGHW VSLNQPLQLV QGLNELTLLS EIVGLQNYGA
     FLEKDGAGFR GQVKLTGLSN GDIDLTNSLW TYQIGLKGEF SRIYSPEYQG SAEWSSMQND
     DTVSPFTWFK TMFDAPEGNG PVTIDLGSMG KGQAWVNGHL IGRYWSLVAP ESGCPSSCNY
     AGTYSDSKCR SNCGIATQSW YHIPREWLQE SGNLLVLFEE TGGDPSQISL EVHYTKTICS
     KISETYYPPL SAWSRAANGR PSVNTVAPEL RLQCDDGHVI SKITFASYGT PTGGCQNFSV
     GNCHASTTLD LVVEACEGKN RCAISVTNEV FGDPCRKVVK DLAVEAECSP PSVNQEPRYD
     I
//
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