ID A0A2C9VEG8_MANES Unreviewed; 833 AA.
AC A0A2C9VEG8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=MANES_08G017800 {ECO:0000313|EMBL:OAY42814.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY42814.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY42814.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY42814.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) 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; CM004394; OAY42814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9VEG8; -.
DR EnsemblPlants; OAY42814; OAY42814; MANES_08G017800.
DR Gramene; OAY42814; OAY42814; MANES_08G017800.
DR OMA; FKNEMQI; -.
DR OrthoDB; 506729at2759; -.
DR Proteomes; UP000091857; Chromosome lg8.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
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:SF160; BETA-GALACTOSIDASE; 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:UP000091857};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..833
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012090191"
FT DOMAIN 748..833
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 833 AA; 94322 MW; 35797072A2D0216E CRC64;
MGFSAIFAAF CLSILCSSLS SAYDVTYDDR AIKIDGQRKL LISGSIHYPR STPGMWPSLI
RKSKEGGLNT IETYVFWNAH EPQPRQYDFA ENLDLVRFIK TIRDEGLYAI LRIGPYVCAE
WDYGGFPIWL HSLPGIKMRT NNDVFKNEMQ IFTTYIVDMM KREGLFASQG GPILLAQIEN
EYGNVQWAYG DDGKKYLDWC AKMADNLKIG IPWVMCQQDD APSPMLSACN GYYCDQWSPK
NSSIPKIWTE NWSGWFMDWG NRVPRRTAED LAFAVARFFQ LGGAVQNYYM YHGGTNFGKS
AGGPYITTSY DYDAPLDEYG NTRQPKWGHL KNLHLTLMSM EEALVYGERT SVDYQNNTYV
TIFAHQGKRS CFFSNTDEKN DRTLTFEGSN YFIPAWSVSI LPDCYTEVYN TAKVNAQTSI
MEKRPNEADD FQEPYALTWQ WKSEKIPHIN ADGILDRSFS FVSNVLMDQK RASNGSSDYL
WLLTNYEHNT SDPQWGNDKD IILHVHTDGH VVHAFVNGKY YGSQWAENGH YEFIFEKRIQ
LKPGNNSITL ASVTVGLPNY GENYDTVRVG IHGPVKLIAR SKTGEPDVKD ISSSRWVYKT
GLIGEDQGLN QVQPRHISQW ETSKLPNNRP FVWYKTSFKG PMGSDPVVVD LLGLGKGVAW
INGRSIGRYW PKYLASEQGC DVICDYRAAY KPEKCNTGCG KPSQRFYHVP RDWLKADDNQ
LVLFEELGGN PYPVNFQTVT VGKVCANAYE GHTLELACHA GSKFSNIKFA SFGLPEGDCG
HFNVGTCHSE KTLSVVQKAC LGKERCVLHV TEDSFGPLRC RADTYRLAVE AVC
//
