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RMLC_SHIFL
ID   RMLC_SHIFL              Reviewed;         181 AA.
AC   P37780;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=dTDP-4-dehydrorhamnose 3,5-epimerase {ECO:0000250|UniProtKB:P26394};
DE            EC=5.1.3.13 {ECO:0000250|UniProtKB:P26394};
DE   AltName: Full=Thymidine diphospho-4-keto-rhamnose 3,5-epimerase {ECO:0000250|UniProtKB:P26394};
DE   AltName: Full=dTDP-4-keto-6-deoxyglucose 3,5-epimerase {ECO:0000250|UniProtKB:P26394};
DE   AltName: Full=dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase {ECO:0000250|UniProtKB:P26394};
DE   AltName: Full=dTDP-L-rhamnose synthase {ECO:0000250|UniProtKB:P26394};
GN   Name=rfbC; Synonyms=rmlC; OrderedLocusNames=SF2101, S2223;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PE577 / Serotype 2a;
RX   PubMed=8170390; DOI=10.1111/j.1365-2958.1994.tb00308.x;
RA   Macpherson D.F., Manning P.A., Morona R.;
RT   "Characterization of the dTDP-rhamnose biosynthetic genes encoded in the
RT   rfb locus of Shigella flexneri.";
RL   Mol. Microbiol. 11:281-292(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YSH6200 / Serotype 2a;
RX   PubMed=8157605; DOI=10.1128/jb.176.8.2362-2373.1994;
RA   Rajakumar K., Jost B.H., Sasakawa C., Okada N., Yoshikawa M., Adler B.;
RT   "Nucleotide sequence of the rhamnose biosynthetic operon of Shigella
RT   flexneri 2a and role of lipopolysaccharide in virulence.";
RL   J. Bacteriol. 176:2362-2373(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of
CC       dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
CC       {ECO:0000250|UniProtKB:P26394}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-
CC         L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649,
CC         ChEBI:CHEBI:62830; EC=5.1.3.13;
CC         Evidence={ECO:0000250|UniProtKB:P26394};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000250|UniProtKB:P26394}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis. {ECO:0000250|UniProtKB:P26394}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P26394}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; X71970; CAA50770.1; -; Genomic_DNA.
DR   EMBL; L14842; AAA53682.1; -; Genomic_DNA.
DR   EMBL; AE005674; AAN43640.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17469.1; -; Genomic_DNA.
DR   PIR; E55213; E55213.
DR   RefSeq; NP_707933.1; NC_004337.2.
DR   RefSeq; WP_001100804.1; NZ_WPGV01000030.1.
DR   AlphaFoldDB; P37780; -.
DR   SMR; P37780; -.
DR   STRING; 198214.SF2101; -.
DR   EnsemblBacteria; AAN43640; AAN43640; SF2101.
DR   EnsemblBacteria; AAP17469; AAP17469; S2223.
DR   GeneID; 1026775; -.
DR   KEGG; sfl:SF2101; -.
DR   KEGG; sfx:S2223; -.
DR   PATRIC; fig|198214.7.peg.2509; -.
DR   HOGENOM; CLU_090940_1_1_6; -.
DR   OMA; RGVFLEW; -.
DR   OrthoDB; 1618609at2; -.
DR   UniPathway; UPA00124; -.
DR   UniPathway; UPA00281; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; ISS:UniProtKB.
DR   GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR000888; dTDP_sugar_isom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR21047; PTHR21047; 1.
DR   Pfam; PF00908; dTDP_sugar_isom; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   TIGRFAMs; TIGR01221; rmlC; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; Lipopolysaccharide biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..181
FT                   /note="dTDP-4-dehydrorhamnose 3,5-epimerase"
FT                   /id="PRO_0000207980"
FT   ACT_SITE        62
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   ACT_SITE        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         47..49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   SITE            138
FT                   /note="Participates in a stacking interaction with the
FT                   thymidine ring of dTDP-4-oxo-6-deoxyglucose"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SFD1"
SQ   SEQUENCE   181 AA;  20823 MW;  25C1DB7591CDB229 CRC64;
     MNVIKTEIPD VLIFEPKVFG DERGFFMESF NQKVFEEAVG RKVEFVQDNH SKSTKGVLRG
     LHYQLEPYAQ GKLVRCVVGE VFDVAVDIRK SSPTFGKWVG VNLSAENKRQ LWIPEGFAHG
     FCVLSDEAEF VYKTNNFYSK MQERGILWSD KSINIEWPVQ NPLLSDKDIN GQKFVDADYF
     I
 
 
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