ID   RAFA_ECOLX              Reviewed;         708 AA.
AC   P16551;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Alpha-galactosidase;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase;
GN   Name=rafA;
OS   Escherichia coli.
OG   Plasmid pRSD2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2556373; DOI=10.1128/jb.171.12.6753-6763.1989;
RA   Aslanidis C., Schmid K., Schmitt R.;
RT   "Nucleotide sequences and operon structure of plasmid-borne genes mediating
RT   uptake and utilization of raffinose in Escherichia coli.";
RL   J. Bacteriol. 171:6753-6763(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX   PubMed=2180920; DOI=10.1128/jb.172.4.2178-2180.1990;
RA   Aslanidis C., Schmitt R.;
RT   "Regulatory elements of the raffinose operon: nucleotide sequences of
RT   operator and repressor genes.";
RL   J. Bacteriol. 172:2178-2180(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-5.
RX   PubMed=786627; DOI=10.1111/j.1432-1033.1976.tb10637.x;
RA   Schmid K., Schmitt R.;
RT   "Raffinose metabolism in Escherichia coli K12. Purification and properties
RT   of a new alpha-galactosidase specified by a transmissible plasmid.";
RL   Eur. J. Biochem. 67:95-104(1976).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC         residues in alpha-D-galactosides, including galactose
CC         oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family. {ECO:0000305}.
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DR   EMBL; M27273; AAA24497.1; -; Genomic_DNA.
DR   EMBL; M29849; AAA24501.1; -; Genomic_DNA.
DR   PIR; A43717; A43717.
DR   RefSeq; WP_000624161.1; NZ_QZWA01000078.1.
DR   AlphaFoldDB; P16551; -.
DR   SMR; P16551; -.
DR   BindingDB; P16551; -.
DR   ChEMBL; CHEMBL4295719; -.
DR   CAZy; GH36; Glycoside Hydrolase Family 36.
DR   PATRIC; fig|562.6988.peg.1499; -.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   CDD; cd14791; GH36; 1.
DR   Gene3D; 2.70.98.60; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR038417; Alpga-gal_N_sf.
DR   InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR   InterPro; IPR002252; Glyco_hydro_36.
DR   InterPro; IPR031705; Glyco_hydro_36_C.
DR   InterPro; IPR031704; Glyco_hydro_36_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF16874; Glyco_hydro_36C; 1.
DR   Pfam; PF16875; Glyco_hydro_36N; 1.
DR   PIRSF; PIRSF005536; Agal; 1.
DR   PRINTS; PR00743; GLHYDRLASE36.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Plasmid.
FT   CHAIN           1..708
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000134873"
FT   ACT_SITE        441
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT   ACT_SITE        505
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
SQ   SEQUENCE   708 AA;  81188 MW;  3D915DA5DB0A202E CRC64;
     MISKYCRLSS PRSDLIIKTH PHAEIIWWGS ALKHFSPDDC ASLERPVANG RLDIDTPLTL
     IAENALGLFS SPGLEGHRNG LDASPVFYTV DVEHTENTLR LTSEDSVAGL RLVSELVMTP
     SGILKVRHAL TNLREGDWQI NRFAITLPVA ERAEEVMAFH GRWTREFQPH RVRLTHDAFV
     LENRRGRTSH EHFPALIVGT PGFSEQQGEV WAVHLGWSGN HRMRCEAKTD GRRYVQAEAL
     WMPGEKALRK NETLYTPWLY ACHSADGLNG MSQQYHRFLR DEIIRFPEQK LRPVHLNTWE
     GIYFNHNPDY IMQMAERAAA LGVERFIIDD GWFKGRNDDR AALGDWYTDE QKYPNGLMPV
     INHVKSLGME FGIWVEPEMI NPDSDLFRLH PDWILSMPGY SQPTGRYQYV LNLNIPEAFD
     YIYKRFLWLL GEHPVDYVKW DMNRELVQAG HEGRAAADAQ TRQFYRLLDL LRERFPHVEF
     ESCASGGGRI DFEVLKRTHR FWASDNNDAL ERCTIQRGMS YFFPPEVMGA HIGHRRCHAT
     FRQHSIAFRG LTALFGHMGL ELDPVAADAK ESDGYRRYAL LYKEWRQLIH TGVLWRVDMP
     DSSIQVQGVV SPDQSQALFM ISQLAMPDYT LPGILRFPGL AAEVRYRLRV IDHPEIQLVG
     EGGHTMRRLP AWMNQPLEAS GEWLAKGGIQ LPVLDPESAI LIALERAV