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AGAL_ECOLI
ID   AGAL_ECOLI              Reviewed;         451 AA.
AC   P06720; Q2M6I5;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Alpha-galactosidase;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase;
GN   Name=melA; Synonyms=mel-7; OrderedLocusNames=b4119, JW4080;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3031590; DOI=10.1093/nar/15.5.2213;
RA   Liljestroem P.L., Liljestroem P.;
RT   "Nucleotide sequence of the melA gene, coding for alpha-galactosidase in
RT   Escherichia coli K-12.";
RL   Nucleic Acids Res. 15:2213-2220(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RX   PubMed=6329200; DOI=10.1016/0006-291x(84)90685-5;
RA   Shimamoto T., Yazyu H., Futai M., Tsuchiya T.;
RT   "Nucleotide sequence of the promoter region of the melibiose operon of
RT   Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 121:41-46(1984).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-20, COFACTOR, AND SUBUNIT.
RX   PubMed=2831880; DOI=10.1016/0006-291x(88)90584-0;
RA   Nagao Y., Nakada T., Imoto M., Shimamoto T., Sakai S., Tsuda M.,
RA   Tsuchiya T.;
RT   "Purification and analysis of the structure of alpha-galactosidase from
RT   Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 151:236-241(1988).
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=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000269|PubMed:2831880};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:2831880};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:2831880};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:2831880};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2831880}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA24149.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X04894; CAA28581.1; -; Genomic_DNA.
DR   EMBL; K01490; AAA24149.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U14003; AAA97019.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77080.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78121.1; -; Genomic_DNA.
DR   PIR; A26571; GBECAG.
DR   RefSeq; NP_418543.1; NC_000913.3.
DR   RefSeq; WP_000986601.1; NZ_SSZK01000018.1.
DR   AlphaFoldDB; P06720; -.
DR   SMR; P06720; -.
DR   BioGRID; 4262685; 8.
DR   DIP; DIP-10179N; -.
DR   IntAct; P06720; 3.
DR   STRING; 511145.b4119; -.
DR   ChEMBL; CHEMBL3696; -.
DR   CAZy; GH4; Glycoside Hydrolase Family 4.
DR   jPOST; P06720; -.
DR   PaxDb; P06720; -.
DR   PRIDE; P06720; -.
DR   EnsemblBacteria; AAC77080; AAC77080; b4119.
DR   EnsemblBacteria; BAE78121; BAE78121; BAE78121.
DR   GeneID; 948636; -.
DR   KEGG; ecj:JW4080; -.
DR   KEGG; eco:b4119; -.
DR   PATRIC; fig|1411691.4.peg.2581; -.
DR   EchoBASE; EB0572; -.
DR   eggNOG; COG1486; Bacteria.
DR   HOGENOM; CLU_045951_1_1_6; -.
DR   InParanoid; P06720; -.
DR   OMA; EHIYHAA; -.
DR   PhylomeDB; P06720; -.
DR   BioCyc; EcoCyc:ALPHAGALACTOSID-MON; -.
DR   BioCyc; MetaCyc:ALPHAGALACTOSID-MON; -.
DR   PRO; PR:P06720; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IDA:EcoCyc.
DR   GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR   GO; GO:0070403; F:NAD+ binding; IDA:EcoCyc.
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:0005995; P:melibiose catabolic process; IMP:EcoCyc.
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   PANTHER; PTHR32092; PTHR32092; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Manganese; Metal-binding; NAD; Reference proteome.
FT   CHAIN           1..451
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000169852"
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;  50657 MW;  CB20367C0860AB5F CRC64;
     MMSAPKITFI GAGSTIFVKN ILGDVFHREA LKTAHIALMD IDPTRLEESH IVVRKLMDSA
     GASGKITCHT QQKEALEDAD FVVVAFQIGG YEPCTVTDFE VCKRHGLEQT IADTLGPGGI
     MRALRTIPHL WQICEDMTEV CPDATMLNYV NPMAMNTWAM YARYPHIKQV GLCHSVQGTA
     EELARDLNID PATLRYRCAG INHMAFYLEL ERKTADGSYV NLYPELLAAY EAGQAPKPNI
     HGNTRCQNIV RYEMFKKLGY FVTESSEHFA EYTPWFIKPG REDLIERYKV PLDEYPKRCV
     EQLANWHKEL EEYKKASRID IKPSREYAST IMNAIWTGEP SVIYGNVRND GLIDNLPQGC
     CVEVACLVDA NGIQPTKVGT LPSHLAALMQ TNINVQTLLT EAILTENRDR VYHAAMMDPH
     TAAVLGIDEI YALVDDLIAA HGDWLPGWLH R
 
 
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