ID F2I9X4_FLUTR Unreviewed; 301 AA. AC F2I9X4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 49. DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082}; DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082}; GN OrderedLocusNames=Fluta_2146 {ECO:0000313|EMBL:AEA44132.1}; OS Fluviicola taffensis (strain DSM 16823 / NCIMB 13979 / RW262). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Crocinitomicaceae; Fluviicola. OX NCBI_TaxID=755732 {ECO:0000313|EMBL:AEA44132.1, ECO:0000313|Proteomes:UP000007463}; RN [1] {ECO:0000313|EMBL:AEA44132.1, ECO:0000313|Proteomes:UP000007463} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16823 / RW262 / RW262 {ECO:0000313|Proteomes:UP000007463}; RX PubMed=22180807; DOI=10.4056/sigs.2124912; RA Woyke T., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G., RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M., RA Mwirichia R., Sikorski J., Tindall B.J., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of the gliding freshwater bacterium Fluviicola RT taffensis type strain (RW262)."; RL Stand. Genomic Sci. 5:21-29(2011). RN [2] {ECO:0000313|Proteomes:UP000007463} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16823 / RW262 / RW262 {ECO:0000313|Proteomes:UP000007463}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I., RA Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Fluviicola taffensis DSM 16823."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002542; AEA44132.1; -; Genomic_DNA. DR RefSeq; WP_013686902.1; NC_015321.1. DR AlphaFoldDB; F2I9X4; -. DR STRING; 755732.Fluta_2146; -. DR KEGG; fte:Fluta_2146; -. DR eggNOG; COG1091; Bacteria. DR HOGENOM; CLU_045518_2_1_10; -. DR OrthoDB; 9803892at2; -. DR UniPathway; UPA00124; -. DR Proteomes; UP000007463; 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 CDD; cd05254; dTDP_HR_like_SDR_e; 1. 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:UP000007463}. FT DOMAIN 1..296 FT /note="RmlD-like substrate binding" FT /evidence="ECO:0000259|Pfam:PF04321" SQ SEQUENCE 301 AA; 33558 MW; 9451CA0772282AC5 CRC64; MKILITGSNG LLGQKIVKRC LKHHISFIAT SKGVNRNPEC PSENYIELDL VNSEEVEALI KAQKPTAIIH TAALTNVDYC ELHPEECYFV NVRASNVLFE AAKKVKAHFQ LLSTDFVFDG ENGPYKEDDT VNPLSIYAQS KVDAEELLLN DSDTNWSIAR TIIVYGTGFG LSRSNMILWA LEALPKGEVM KLVDDQFRAP TWADDLAYGC VEIIKRNERG IFHLSGPVTR SVKAIVEEVG KALELENIAI ETISSTTLNQ AAKRPPRTGF DLSKAAQKLD YLPLDIQESI PLLLRDIDYY S //