ID A0A653A6X8_9DELT Unreviewed; 294 AA. AC A0A653A6X8; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 17-JUN-2020, entry version 2. DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082}; DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082}; GN Name=strL {ECO:0000313|EMBL:VBB43734.1}; GN ORFNames=TRIP_B310042 {ECO:0000313|EMBL:VBB43734.1}; OS uncultured Desulfatiglans sp. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfatiglans; environmental samples. OX NCBI_TaxID=1748965 {ECO:0000313|EMBL:VBB43734.1}; RN [1] {ECO:0000313|EMBL:VBB43734.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IK1 {ECO:0000313|EMBL:VBB43734.1}; RG Genoscope - CEA; RA William W.; RL Submitted (JUL-2018) 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU364082}; CC Note=Binds 1 Mg(2+) ion per monomer. {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|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; UPXX01000025; VBB43734.1; -; Genomic_DNA. DR UniPathway; UPA00124; -. DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC. DR InterPro; IPR005913; dTDP_dehydrorham_reduct. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR029903; RmlD-like-bd. DR PANTHER; PTHR10491; PTHR10491; 1. DR Pfam; PF04321; RmlD_sub_bind; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01214; rmlD; 1. PE 3: Inferred from homology; KW NADP {ECO:0000256|RuleBase:RU364082}; KW Oxidoreductase {ECO:0000256|RuleBase:RU364082, KW ECO:0000313|EMBL:VBB43734.1}. FT DOMAIN 4..282 FT /note="RmlD_sub_bind" FT /evidence="ECO:0000259|Pfam:PF04321" SQ SEQUENCE 294 AA; 32402 MW; E4852EDE7503816A CRC64; MKKQVLICGG AGQLGRDCAA VLEAAWRVSA PGSKTLDIAD REAVLEAVEA LRPDVILNCA AYTKVDQCET DRAEAWRVNA LGPRNLAEAG ATHGALLVHV STDYVFDGRR VPPEPYTEED APGPLSVYGQ SKLAGEMAVR EIAERHAILR TAWLYGAGGH NFLKTMLRLA VSDPERVIRV VNDQYGCPTW SRDLARQIAR VMEAGVCGTF HACGEGFCTW YDLARRFLEL MALPHRLAPC STSEYPTAAV RPRNSILENR RLKEEGLDVM RPWEEALEEF VALNGRALLE EVNA //