ID V7C958_PHAVU Unreviewed; 833 AA.
AC V7C958;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=PHAVU_003G137000g {ECO:0000313|EMBL:ESW26654.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW26654.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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; CM002290; ESW26654.1; -; Genomic_DNA.
DR RefSeq; XP_007154660.1; XM_007154598.1.
DR AlphaFoldDB; V7C958; -.
DR EnsemblPlants; ESW26654; ESW26654; PHAVU_003G137000g.
DR GeneID; 18634834; -.
DR Gramene; ESW26654; ESW26654; PHAVU_003G137000g.
DR KEGG; pvu:PHAVU_003G137000g; -.
DR eggNOG; KOG0496; Eukaryota.
DR OMA; RGNCGNC; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000000226; Chromosome 3.
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:SF63; BETA-GALACTOSIDASE 12; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 2.
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:UP000000226};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..833
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004755398"
FT DOMAIN 747..833
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 833 AA; 92532 MW; 5B770BEEF9ACDF58 CRC64;
MENLPRGIFY SLLLFLWVCA VTASVTYDHK AILVNGQRRI LVSGSIHYPR STPEMWPDLI
QKAKDGGLDV IETYVFWNGH EPSPGKYYFE DRYDLVKFIK VVQQAGLYLH LRIGPFVCAE
WNFGGFPVWL KYVPGIAFRT DNEPFKAAMQ NFTEKIVSMM KEEKLFQTEG GPIIMSQIEN
EFGPVEWEIG APGKAYAQWA AKMAVGLDTG VPWIMCKQED APDPVINTCN GYYCENFTPN
KEYKPKMWTE NWSGWYTEFG GAVPRRPAED MAFSVARFVQ NGGSFVNYYM FHGGTNFDRT
SGGPFIATSY DYDGLLDEYG LLNEPKWGHL RDLHKAIKLC EAALVSVDPT VTWPGKNLEV
HVFKTSGACA AFLANYDTKS SATVTFENGQ YDLPPWSISI LPDCKTEVFN TARVGAQSSL
MKMTAVNTAF DWQSYNEEPA SSSEDDPLTA YALWEQINIT RDSTDYLWYM TDVNIDANEG
FIKSGQSPVL TVMSAGHALH VFINGQLSGT VYGGLEFPKL TFSDGVKLRV GNNKISLLSI
AVGLPNVGTH FETWNAGVLG PVTLNGLNEG TRDLSKQKWS YKIGLKGEAL NLNTVSGSSS
VEWVQGSLLA KKQPLTWYKT TFSTPVGNDP LALDMISMGK GQVWINGRSI GRHWPGYIAR
GHCGECYYAG TYNDKKCRTN CGEPSQRWYH IPRSWLNPSG NYLVVLEEWG GDPNGISLVK
RTTASVCADI YEGQPTLKSR HMLDTGKINR PKAHLWCPPG LKISQIKFAS YGLPQGTCGN
YREGSCHAHR SYDAPEKNCI GKQSCSVTVA PEVFGGDPCP GTAKKLSLEA LCS
//
