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Database: UniProt
Entry: V7AYS1_PHAVU
LinkDB: V7AYS1_PHAVU
Original site: V7AYS1_PHAVU 
ID   V7AYS1_PHAVU            Unreviewed;       843 AA.
AC   V7AYS1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
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_009G153100g {ECO:0000313|EMBL:ESW09748.1};
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:ESW09748.1, 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; CM002296; ESW09748.1; -; Genomic_DNA.
DR   RefSeq; XP_007137754.1; XM_007137692.1.
DR   AlphaFoldDB; V7AYS1; -.
DR   STRING; 3885.V7AYS1; -.
DR   EnsemblPlants; ESW09748; ESW09748; PHAVU_009G153100g.
DR   GeneID; 18620247; -.
DR   Gramene; ESW09748; ESW09748; PHAVU_009G153100g.
DR   KEGG; pvu:PHAVU_009G153100g; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   OMA; NGTHSPF; -.
DR   OrthoDB; 5489808at2759; -.
DR   Proteomes; UP000000226; Chromosome 9.
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; 1.
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:SF67; BETA-GALACTOSIDASE 10; 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; PS51257; PROKAR_LIPOPROTEIN; 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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..843
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004754251"
FT   DOMAIN          761..843
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   843 AA;  93655 MW;  E73B137435923F0D CRC64;
     MKFCLLGAVL LLTVTVASCG NVSYDGRSLI IDGQRKLLIS ASIHYPRSVP AMWPGLVQTA
     KEGGVDVIET YVFWNGHELS PGNYYFGGRF DLVKFAKTVQ QAGMFLILRI GPFVAAEWNF
     GGVPVWLHYV PGTVFRTYNQ PFMYHMQKFT TYIVNLMKQE KLFASQGGPI ILAQIENEYG
     YYENFYKENG KKYALWAAKM AVSQNTGVPW IMCQQWDAPD PVIDTCNSFY CDQFKPTSPN
     RPKIWTENWP GWFKTFGGRD PHRPAEDVAF SVARFFQKGG SVHNYYMYHG GTNFGRTAGG
     PFITTSYDYD APIDEYGLPR LPKWDHLKEL HRAIKLCEHA LLNGKSVNVS LGPSVEVDVY
     TDSSGACAAF ISNADDKNDR TVEFRNTSYH LPAWSVSILP DCKNVVFNTA KVSSQTNVVA
     MIPGSLQQSN KGVNSLKWDI VKEKPGIWGT ADFVKNGFVD LINTTKDTTD YLWHTTSISV
     GENEEFLKKG SKPVLLIEST GHALHAFVNQ EYQGTGTGNG THSPFTFKNP ISLRAGKNEI
     ALLCLTVGLQ TAGPFYDFVG AGLTSVKIEG LNNGTIDLSS YAWTYKIGVQ GEHLKLNQGD
     GLNNVNWTST SEPPKMQPLT WYKAIVDAPP GDEPVGLDML HMGKGLAWLN GEEIGRYWPR
     KSEFKSEDCV KECDYRGKFN PDKCDTGCGE PTQRWYHVPR SWFKPSGNIL VLFEEKGGEP
     DKIRFVRRKI SGACALVAED YPSVGLLSQG EDKIQNNKNI PFARLTCPSN THISAVKFAS
     FGTPSGSCGS YLKGDCHDPN SSIVVEKACL NKNDCVIKLT EENFKTNLCP GLSRKLAVEA
     ICS
//
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