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AGAL_RHIME
ID   AGAL_RHIME              Reviewed;         490 AA.
AC   Q9X4Y0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Alpha-galactosidase;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase;
GN   Name=melA; OrderedLocusNames=RB1568; ORFNames=SMb21648;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymB (megaplasmid 2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=9791127; DOI=10.1128/jb.180.21.5739-5748.1998;
RA   Gage D.J., Long S.R.;
RT   "Alpha-galactoside uptake in Rhizobium meliloti: isolation and
RT   characterization of agpA, a gene encoding a periplasmic binding protein
RT   required for melibiose and raffinose utilization.";
RL   J. Bacteriol. 180:5739-5748(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481431; DOI=10.1073/pnas.161294698;
RA   Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA   Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT   "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT   endosymbiont Sinorhizobium meliloti.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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; AF119834; AAD26273.1; -; Genomic_DNA.
DR   EMBL; AL591985; CAC49967.1; -; Genomic_DNA.
DR   PIR; G96037; G96037.
DR   RefSeq; NP_438107.1; NC_003078.1.
DR   RefSeq; WP_003527988.1; NC_003078.1.
DR   AlphaFoldDB; Q9X4Y0; -.
DR   SMR; Q9X4Y0; -.
DR   STRING; 266834.SM_b21648; -.
DR   CAZy; GH4; Glycoside Hydrolase Family 4.
DR   EnsemblBacteria; CAC49967; CAC49967; SM_b21648.
DR   GeneID; 61601471; -.
DR   KEGG; sme:SM_b21648; -.
DR   PATRIC; fig|266834.11.peg.6494; -.
DR   eggNOG; COG1486; Bacteria.
DR   HOGENOM; CLU_045951_1_1_5; -.
DR   OMA; NEHASHI; -.
DR   Proteomes; UP000001976; Plasmid pSymB.
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   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   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Manganese; Metal-binding;
KW   NAD; Plasmid; Reference proteome.
FT   CHAIN           1..490
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000169853"
FT   ACT_SITE        172
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        258
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         4..70
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   490 AA;  54605 MW;  B68698CF901F6BCD CRC64;
     MASFKIAIIG AGSIGFTKKL FTDILSVPEL RDVEFALTDL SEHNLAMIKS ILDRIVEANE
     LPTRVTATTD RRKALEGARY IISCVRVGGL EAYADDIRIP LKYGVDQCVG DTICAGGILY
     GQRNIPVILD FCKDIREVAE PGAKFLNYAN PMAMNTWAAI EYGKVDTVGL CHGVQHGAEQ
     IAEILGARDG ELDYICSGIN HQTWFVDVRL NGRKVGKDEL VAAFEAHPVF SKQEKLRIDV
     LKRFGVYSTE SNGHLSEYLP WYRKRPDEIS RWIDMSDWIH GETGGYLRYS TETRNWFETE
     YPRFLEEAGR PLETIRRSNE HASRILEALE TGRVYRGHFN VKNNGVITNL PADAIIESPG
     FVDRFGINMV AGITLPEACA ATCISSVNVQ RMSVHAAITG DIDLLKLAVL HDPLVGAICT
     PEEVWQMVDE MVVAQAKWLP QYAHAIDAAK ERLARATVAT REWKGAARRE VRSIEEIRAE
     KEAAKLRAAG
 
 
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