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RFBJ_SALMU
ID   RFBJ_SALMU              Reviewed;         293 AA.
AC   Q00329;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=CDP-abequose synthase {ECO:0000303|PubMed:1379320};
DE            EC=1.1.1.341 {ECO:0000250|UniProtKB:P0A1P4};
GN   Name=rfbJ {ECO:0000303|PubMed:1379320};
OS   Salmonella muenchen.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M67;
RX   PubMed=1379320; DOI=10.1111/j.1365-2958.1992.tb00859.x;
RA   Brown P.K., Romana L.K., Reeves P.R.;
RT   "Molecular analysis of the rfb gene cluster of Salmonella serovar muenchen
RT   (strain M67): the genetic basis of the polymorphism between groups C2 and
RT   B.";
RL   Mol. Microbiol. 6:1385-1394(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP-alpha-D-abequose + NADP(+) = CDP-4-dehydro-3,6-dideoxy-
CC         alpha-D-glucose + H(+) + NADPH; Xref=Rhea:RHEA:34563,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:70783, ChEBI:CHEBI:70784; EC=1.1.1.341;
CC         Evidence={ECO:0000250|UniProtKB:P0A1P4};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; X61917; CAA43918.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q00329; -.
DR   SMR; Q00329; -.
DR   UniPathway; UPA00281; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Lipopolysaccharide biosynthesis; NADP; Oxidoreductase.
FT   CHAIN           1..293
FT                   /note="CDP-abequose synthase"
FT                   /id="PRO_0000183258"
FT   ACT_SITE        130
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  33775 MW;  F7EE8187B2E87B17 CRC64;
     MLDVNKKILM TGATSFVGTH LLHSLIKEGY SIIALKRPIT EPTIINTLIE WLNIQDIEKI
     CQSSMNIHAI VHIATDYGRN RTPISEQYKC NVLLPTRLLE LMPALKTKFF ISTDSFFGKY
     EKHYGYMRSY MASKRHFVEL SKIYVEEHPD VCFINLRLEH VYGERDKAGK IIPYVIKKMK
     NNEDIDCTIA RQKRDFIYID DVVSAYLKIL KEGFNAGHYD VEVGTGKSIE LKEVFEIIKK
     ETHSSSKINY GAVAMRDDEI MESHANTSFL TRLGWSAEFS IEKGVKKMLS MKE
 
 
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