ID   BGAL_DIACA              Reviewed;         731 AA.
AC   Q00662;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Putative beta-galactosidase;
DE            Short=Lactase;
DE            EC=3.2.1.23;
DE   AltName: Full=SR12 protein;
DE   Flags: Precursor;
GN   Name=CARSR12;
OS   Dianthus caryophyllus (Carnation) (Clove pink).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus.
OX   NCBI_TaxID=3570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. White Sim; TISSUE=Petal;
RX   PubMed=1868223; DOI=10.1007/bf00036806;
RA   Raghothama K.G., Lawton K.A., Goldsbrough P.B., Woodson W.R.;
RT   "Characterization of an ethylene-regulated flower senescence-related gene
RT   from carnation.";
RL   Plant Mol. Biol. 17:61-71(1991).
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   -!- TISSUE SPECIFICITY: Senescing flower petals.
CC   -!- INDUCTION: By ethylene.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; X57171; CAA40459.1; -; Genomic_DNA.
DR   PIR; S16595; S16595.
DR   AlphaFoldDB; Q00662; -.
DR   SMR; Q00662; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; PTHR23421; 1.
DR   Pfam; PF17834; GHD; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..731
FT                   /note="Putative beta-galactosidase"
FT                   /id="PRO_0000012196"
FT   ACT_SITE        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        257
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   731 AA;  82864 MW;  83FA8B5A3779C051 CRC64;
     MLCGKENNVM KMMLVYVFVL ITLISCVYGN VWYDYRAIKI NDQRRILLSG SIHYPRSTPE
     MWPDIIEKAK DSQLDVIQTY VFWNGHEPSE GKYYFEGRYD LVKFIKLIHQ AGLFVHLRIG
     PFACAEWNFG GFPVWLKYVP GIEFRTDNGP FKEKMQVFTT KIVDMMKAEK LFHWQGGPII
     LNQIENEYGP VEWEIGAPGK AYTHWAAQMA QSLNAGVPWI MCKQDSDVPD NVIDTCNGFY
     CEGFVPKDKS KPKMWTENWT GWYTEYGKPV PYRPAEDVAF SVARFIQNGG SFMNYYMFHG
     GTNFETTAGR FVSTSYDYDA PLDEYGLPRE PKYTHLKNLH KAIKMCEPAL VSSDAKVTNL
     GSNQEAHVYS SNSGSCAAFL ANYDPKWSVK VTFSGMEFEL PAWSISILPD CKKEVYNTAR
     VNEPSPKLHS KMTPVISNLN WQSYSDEVPT ADSPGTFREK KLYEQINMTW DKSDYLWYMT
     DVVLDGNEGF LKKGDEPWLT VNSAGHVLHV FVNGQLQGHA YGSLAKPQLT FSQKVKMTAG
     VNRISLLSAV VGLANVGWHF ERYNQGVLGP VTLSGLNEGT RDLTWQYWSY KIGTKGEEQQ
     VYNSGGSSHV QWGPPAWKQP LVWYKTTFDA PGGNDPLALD LGSMGKGQAW INGQSIGRHW
     SNNIAKGSCN DNCNYAGTYT ETKCLSDCGK SSQKWYHVPR SWLQPRGNLL VVFEEWGGDT
     KWVSLVKRTI A