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YDJC_RHIML
ID   YDJC_RHIML              Reviewed;         293 AA.
AC   P49306;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Carbohydrate deacetylase {ECO:0000250|UniProtKB:Q53WD3};
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q53WD3};
OS   Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=L5-30;
RX   PubMed=7845353; DOI=10.1007/bf00279746;
RA   Rossbach S., Kulpa D.A., Rossbach U., de Bruijn F.J.;
RT   "Molecular and genetic characterization of the rhizopine catabolism
RT   (mocABRC) genes of Rhizobium meliloti L5-30.";
RL   Mol. Gen. Genet. 245:11-24(1994).
CC   -!- FUNCTION: Probably catalyzes the deacetylation of acetylated
CC       carbohydrates an important step in the degradation of oligosaccharides.
CC       {ECO:0000250|UniProtKB:Q53WD3}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q53WD3};
CC   -!- SIMILARITY: Belongs to the YdjC deacetylase family. {ECO:0000305}.
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DR   EMBL; X78503; CAA55268.1; -; Genomic_DNA.
DR   PIR; S51571; S51571.
DR   RefSeq; WP_014528468.1; NZ_WISV01000218.1.
DR   AlphaFoldDB; P49306; -.
DR   SMR; P49306; -.
DR   PATRIC; fig|382.53.peg.1558; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR006879; YdjC-like.
DR   PANTHER; PTHR31609; PTHR31609; 1.
DR   Pfam; PF04794; YdjC; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..293
FT                   /note="Carbohydrate deacetylase"
FT                   /id="PRO_0000160649"
FT   BINDING         73
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q53WD3"
FT   BINDING         144
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q53WD3"
SQ   SEQUENCE   293 AA;  32309 MW;  2D4A662356EAA2D9 CRC64;
     MTSVEKSDSG ECGTPFVVVN IDDVGMCHGA NKAYLELRRL GAVDSGSVMV PCPWFPEIAE
     AGALKPDLNV GIHLTLTSEK RHYRWRPLTK ATPASGLIDS DGFMWRSVAE LRRNAHPDAV
     EAEMRAQIET FLAAGLIPSH VDGHMGGVFA PEFVDRYVAL SLEFKLPTLF PATIEAYGPK
     HNLGAVDQDS YASAAERLLN AGEKLATKAL ETPWHRNQPA LERYQDLYHQ IEPGLNFLCL
     HANAAGEIEA IEPDSAQIRI DEYELLKDPS FLDWADSLSL RRGSLRDARA TSR
 
 
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