ID   A7ZRF0_ECO24            Unreviewed;       708 AA.
AC   A7ZRF0;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   02-SEP-2026, entry version 87.
DE   RecName: Full=Alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
DE            EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
GN   Name=rafA {ECO:0000313|EMBL:ABV20016.1};
GN   OrderedLocusNames=EcE24377A_3380 {ECO:0000313|EMBL:ABV20016.1};
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV20016.1, ECO:0000313|Proteomes:UP000001122};
RN   [1] {ECO:0000313|Proteomes:UP000001122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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         Evidence={ECO:0000256|ARBA:ARBA00001255,
CC         ECO:0000256|PIRNR:PIRNR005536};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase.
CC       {ECO:0000256|PIRNR:PIRNR005536}.
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DR   EMBL; CP000800; ABV20016.1; -; Genomic_DNA.
DR   RefSeq; WP_000253907.1; NC_009801.1.
DR   AlphaFoldDB; A7ZRF0; -.
DR   KEGG; ecw:EcE24377A_3380; -.
DR   HOGENOM; CLU_009640_3_1_6; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   CDD; cd14791; GH36; 1.
DR   FunFam; 3.20.20.70:FF:000118; Alpha-galactosidase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.70.98.60; alpha-galactosidase from lactobacil brevis; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR038417; Alpga-gal_N_sf.
DR   InterPro; IPR050985; Alpha-glycosidase_related.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR   InterPro; IPR002252; Glyco_hydro_36.
DR   InterPro; IPR031704; Glyco_hydro_36_N.
DR   PANTHER; PTHR43053:SF3; ALPHA-GALACTOSIDASE C-RELATED; 1.
DR   PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR   Pfam; PF16875; Glyco_hydro_36N; 1.
DR   Pfam; PF02065; Melibiase; 1.
DR   PIRSF; PIRSF005536; Agal; 1.
DR   PRINTS; PR00743; GLHYDRLASE36.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR005536};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005536};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001122}.
FT   DOMAIN          23..236
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   ACT_SITE        441
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        505
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         329..330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         406
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         439..443
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         483
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         505
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ   SEQUENCE   708 AA;  81138 MW;  AD9D7D1DB18E1214 CRC64;
     MVSKYCRLSS PRSDLIIKTR PHAEIIWWGS ALKHFSPDDC ASLERPVANG RLDIDTPLTL
     MAENALGLFS SPGLEGHRNG LDASPVFYTV DVEHTENTLR LTSEDSVAGL RLVSELVMTP
     SGILKVRHAL TNLREGDWQI NRFAITLPLA ERAEEVMAFH GRWTREFQPH RVRLTHDAFV
     LENRRGRTSH EHFPALIVGT PGFSEQQGEV WAVHLGWSGN HRMRCEAKTD GRRYVQAEAL
     WMPGEKALRK NETLYTPWLY ACHSADGLNG MSQQYHRFLR DEIIRFPEQK PRPVHLNTWE
     GIYFNHNPDY IMQMAERAAA LGVERFIIDD GWFKGRNDDR AALGDWYTDE QKYPNGLMPV
     IKHVKSLGME FGIWVEPEMI NPDSDLFRLH PDWVLSMPGY SQPTGRYQYV LNLNIPEAFA
     YIYERFLWLL GEHPVDYVKW DMNRELVQAG HEGRAAADAQ TRQFYRLLDL LRERFPHVEF
     ESCASGGGRI DFEVLKRTHR FWASDNNDAL ERCTIQRGMS YFFPPEVMGA HIGHRRCHAT
     FRQHSIAFRG LTALFGHMGL ELDPVAADAK ESDGYRRYAL LYKEWRQLIH TGVLWRVDMP
     DPSIQVQGVV SPDQSQALFM ISQLAMPDYT LPGILRFPGL AAEVRYRLRV IDHPDLQVVG
     EGGHTMRKLP VWMNQSLEAS GEWLAQGGIQ LPVLDPESAI LIALERAV
//