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Database: UniProt
Entry: P30877
LinkDB: P30877
Original site: P30877 
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   26-NOV-2014, entry version 98.
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:
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.
CC       {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_003197.1.
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; EDLYPEI; -.
DR   OrthoDB; EOG6CP3SG; -.
DR   PhylomeDB; P30877; -.
DR   BioCyc; SENT99287:GCTI-4329-MONOMER; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:UniProtKB-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; SSF56327; 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. {ECO:0000250}.
FT   ACT_SITE    174    174       Proton donor. {ECO:0000250}.
FT   METAL       173    173       Manganese. {ECO:0000250}.
FT   METAL       203    203       Manganese. {ECO:0000250}.
FT   BINDING     151    151       Substrate. {ECO:0000250}.
FT   BINDING     287    287       Substrate. {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
//
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