ID C1CY77_DEIDV Unreviewed; 250 AA.
AC C1CY77;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN OrderedLocusNames=Deide_20253 {ECO:0000313|EMBL:ACO47033.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47033.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO47033.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
CC -!- FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to
CC yield dTDP-L-rhamnose. {ECO:0000256|RuleBase:RU364082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-
CC rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:21796, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:62830; EC=1.1.1.133;
CC Evidence={ECO:0000256|RuleBase:RU364082};
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000256|RuleBase:RU364082}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC {ECO:0000256|ARBA:ARBA00010944, ECO:0000256|RuleBase:RU364082}.
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DR EMBL; CP001114; ACO47033.1; -; Genomic_DNA.
DR RefSeq; WP_012694154.1; NC_012526.1.
DR AlphaFoldDB; C1CY77; -.
DR STRING; 546414.Deide_20253; -.
DR PaxDb; 546414-Deide_20253; -.
DR KEGG; ddr:Deide_20253; -.
DR eggNOG; COG1091; Bacteria.
DR HOGENOM; CLU_045518_4_0_0; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000002208; Chromosome.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208}.
FT DOMAIN 5..147
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 250 AA; 27398 MW; 3C1E7FB5F5D18FF8 CRC64;
MTAPRILLTG GGGRLGTELQ ALLPNIVAPS SRELDVTNSA QVLEMVWCKR PEVIVHAAAY
TNVGGAEEDR ETCWRVNVEG TRHMAQAANE VGAKLVQIST DYVFSGAQGD YRETDIPGPP
VNYYALTKLV AEEAARTAGQ HLIVRTSFRP REFQYPVAFS DVYTGQDYVD IIAPLVAEAV
LHALEIPDSV LHIVTERKSV FDLARRRNPA VREGRRADVT VPLPADVSLN TDRWQALRAN
WATLGGIPVV
//
