ID   AGAL_SALTY              Reviewed;         451 AA.
AC   P30877;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 2.
DT   02-SEP-2026, entry version 139.
DE   RecName: Full=Alpha-galactosidase;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase;
GN   Name=melA; OrderedLocusNames=STM4298;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 409-451.
RC   STRAIN=LT2;
RX   PubMed=1495487; DOI=10.1007/bf00272347;
RA   Mizushima K., Awakihara S., Kuroda M., Ishikawa T., Tsuda M., Tsuchiya T.;
RT   "Cloning and sequencing of the melB gene encoding the melibiose permease of
RT   Salmonella typhimurium LT2.";
RL   Mol. Gen. Genet. 234:74-80(1992).
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
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DR   EMBL; AE006468; AAL23122.1; -; Genomic_DNA.
DR   EMBL; X62101; CAA44010.1; -; Genomic_DNA.
DR   PIR; S42852; S42852.
DR   RefSeq; NP_463163.1; NC_003197.2.
DR   RefSeq; WP_001520868.1; NC_003197.2.
DR   AlphaFoldDB; P30877; -.
DR   SMR; P30877; -.
DR   STRING; 99287.STM4298; -.
DR   PaxDb; 99287-STM4298; -.
DR   DNASU; 1255824; -.
DR   GeneID; 1255824; -.
DR   KEGG; stm:STM4298; -.
DR   PATRIC; fig|99287.12.peg.4520; -.
DR   HOGENOM; CLU_045951_1_1_6; -.
DR   OMA; EHNAEYH; -.
DR   PhylomeDB; P30877; -.
DR   BioCyc; SENT99287:STM4298-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IBA:GO_Central.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05297; GH4_alpha_glucosidase_galactosidase; 1.
DR   FunFam; 3.90.1820.10:FF:000001; Alpha-galactosidase; 1.
DR   Gene3D; 3.90.1820.10; AglA-like glucosidase; 1.
DR   InterPro; IPR053715; GH4_Enzyme_sf.
DR   InterPro; IPR019802; GlycHydrolase_4_CS.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; NF011657; PRK15076.1; 1.
DR   PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR   PANTHER; PTHR32092:SF6; ALPHA-GALACTOSIDASE; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Manganese; Metal-binding;
KW   NAD; Reference proteome.
FT   CHAIN           1..451
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000169854"
FT   ACT_SITE        174
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         5..71
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   451 AA;  50735 MW;  5106CDC87E3334DF CRC64;
     MMTAPKITFI GAGSTIFVKN ILGDVFHREA LKSAHVALMD IDETRLEESH IVVRKLMDSA
     GASGRITCHT NQKAALQDAD FVVVAFQIGG YEPCTVTDFE VCKRHGLEQT IADTLGPGGI
     MRALRTIPHL WRICEDMTEV CPKATMLNYV NPMAMNTWAM YARYPHIKQV GLCHSVQGTA
     EELARDLNID PTSLRYRCAG INHMAFYLEL ERKTADGTYV NLYPELLAAY DAGQAPKPNI
     HGNERCQNIV RYEMFKKLGY FVTESSEHFA EYTPWFIKPG REDLIARYKV PLDEYPKRCV
     EQLANWHKEL EEYKTAERID IKPSREYAST IMNALWTGEP SVIYGNVRNE GLIDNLPQGS
     CVEVACLVDA NGIQPTKVGT IPSHLAAMMQ TNINVQTLLT EAILTENRDR VYHAAMMDPH
     TAAVLGIEEI YALVDDLIAA HGDWLPAWLR R
//