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 01-MAY-2013, entry version 91.
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; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC 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.,
RA Waterston R., Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 409-451.
RC STRAIN=LT2;
RX PubMed=1495487;
RA Mizushima K., Awakihara S., Kuroda M., Ishikawa T., Tsuda M.,
RA Tsuchiya T.;
RT "Cloning and sequencing of the melB gene encoding the melibiose
RT permease of Salmonella typhimurium LT2.";
RL Mol. Gen. Genet. 234:74-80(1992).
CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing alpha-D-
CC galactose residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.
CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 NAD per subunit (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
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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_003197.1.
DR ProteinModelPortal; P30877; -.
DR STRING; 99287.STM4298; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR PaxDb; P30877; -.
DR PRIDE; P30877; -.
DR EnsemblBacteria; AAL23122; AAL23122; STM4298.
DR GeneID; 1255824; -.
DR KEGG; stm:STM4298; -.
DR PATRIC; 32387505; VBISalEnt20916_4520.
DR eggNOG; COG1486; -.
DR HOGENOM; HOG000239812; -.
DR KO; K07406; -.
DR OMA; GWNPRCP; -.
DR ProtClustDB; PRK15076; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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:0052692; F:raffinose alpha-galactosidase activity; IEA:EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; -; 1.
DR Gene3D; 3.90.110.10; -; 1.
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; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF56327; Lactate_DH/Glyco_hydro_4_C; 1.
DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Complete proteome; Glycosidase; Hydrolase;
KW Manganese; Metal-binding; NAD; Reference proteome.
FT CHAIN 1 451 Alpha-galactosidase.
FT /FTId=PRO_0000169854.
FT NP_BIND 5 71 NAD (By similarity).
FT ACT_SITE 174 174 Proton donor (By similarity).
FT METAL 173 173 Manganese (By similarity).
FT METAL 203 203 Manganese (By similarity).
FT BINDING 151 151 Substrate (By similarity).
FT BINDING 287 287 Substrate (By similarity).
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
//
