RMLC_SINFN
ID RMLC_SINFN Reviewed; 195 AA.
AC P55468;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 OrderedLocusNames=NGR_a03520; ORFNames=y4gL;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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 -!- 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; U00090; AAB91686.1; -; Genomic_DNA.
DR RefSeq; NP_443874.1; NC_000914.2.
DR AlphaFoldDB; P55468; -.
DR SMR; P55468; -.
DR STRING; 394.NGR_a03520; -.
DR EnsemblBacteria; AAB91686; AAB91686; NGR_a03520.
DR KEGG; rhi:NGR_a03520; -.
DR PATRIC; fig|394.7.peg.360; -.
DR eggNOG; COG1898; Bacteria.
DR HOGENOM; CLU_090940_1_1_5; -.
DR OMA; RGVFLEW; -.
DR OrthoDB; 1618609at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
DR GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019305; P:dTDP-rhamnose 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; Plasmid; Reference proteome.
FT CHAIN 1..195
FT /note="dTDP-4-dehydrorhamnose 3,5-epimerase"
FT /id="PRO_0000207982"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 54..56
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT SITE 146
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 195 AA; 21852 MW; 77176926984CC1A2 CRC64;
MGGTELDEMY FQSLSIAEVK LIRPRKFGDC RGYFSEVFRE KWFRKNVADV GLVQDNESLS
AQIGTVRGLH FQLEPFAQGK LVRCTRGALF DVAVDVRVGS PTYGKWVSAE LSQENGAQLW
VPAGFAHGFM TLKADTVISY KVTAPYSAEH DRGLKWDDPA IGINWPKMTT YVLSEKDSSQ
PSLCELPVSF QYVKV
