ID RMLD_MYCS2 Reviewed; 327 AA. AC A0QTF8; I7G6I9; DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000250|UniProtKB:P26392}; DE EC=1.1.1.133 {ECO:0000250|UniProtKB:P26392}; DE AltName: Full=dTDP-4-keto-L-rhamnose reductase {ECO:0000250|UniProtKB:P26392}; DE AltName: Full=dTDP-6-deoxy-L-lyxo-4-hexulose reductase {ECO:0000303|PubMed:12029057}; DE AltName: Full=dTDP-6-deoxy-L-mannose dehydrogenase {ECO:0000250|UniProtKB:P26392}; DE AltName: Full=dTDP-L-rhamnose synthase {ECO:0000250|UniProtKB:P26392}; GN Name=rmlD {ECO:0000303|PubMed:12029057}; Synonyms=rfbD; GN OrderedLocusNames=MSMEG_1825, MSMEI_1782; OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium OS smegmatis). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=246196; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20; RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.; RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic RT mutations or sequencing errors?"; RL Genome Biol. 8:R20.1-R20.9(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=18955433; DOI=10.1101/gr.081901.108; RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.; RT "Ortho-proteogenomics: multiple proteomes investigation through orthology RT and a new MS-based protocol."; RL Genome Res. 19:128-135(2009). RN [4] RP FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS, AND PATHWAY. RX PubMed=12029057; DOI=10.1128/jb.184.12.3392-3395.2002; RA Ma Y., Pan F., McNeil M.; RT "Formation of dTDP-rhamnose is essential for growth of mycobacteria."; RL J. Bacteriol. 184:3392-3395(2002). CC -!- FUNCTION: Involved in the biosynthesis of the dTDP-L-rhamnose which is CC a component of the critical linker, D-N-acetylglucosamine-L-rhamnose CC disaccharide, which connects the galactan region of arabinogalactan to CC peptidoglycan via a phosphodiester linkage (PubMed:12029057). Catalyzes CC the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L- CC rhamnose (By similarity). {ECO:0000250|UniProtKB:P26392, CC ECO:0000269|PubMed:12029057}. 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:0000250|UniProtKB:P26392}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P26392}; CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250|UniProtKB:P26392}; CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. CC {ECO:0000305|PubMed:12029057}. CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AFP38254.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; CP000480; ABK74972.1; -; Genomic_DNA. DR EMBL; CP001663; AFP38254.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_886196.1; NC_008596.1. DR AlphaFoldDB; A0QTF8; -. DR SMR; A0QTF8; -. DR STRING; 246196.MSMEG_1825; -. DR PaxDb; 246196-MSMEI_1782; -. DR KEGG; msg:MSMEI_1782; -. DR KEGG; msm:MSMEG_1825; -. DR PATRIC; fig|246196.19.peg.1807; -. DR eggNOG; COG1091; Bacteria. DR OrthoDB; 9803892at2; -. DR UniPathway; UPA00124; -. DR Proteomes; UP000000757; Chromosome. DR Proteomes; UP000006158; Chromosome. DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IGI:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IGI:UniProtKB. DR CDD; cd05254; dTDP_HR_like_SDR_e; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1. DR InterPro; IPR005913; dTDP_dehydrorham_reduct. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR029903; RmlD-like-bd. DR NCBIfam; TIGR01214; rmlD; 1. 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 1: Evidence at protein level; KW Carbohydrate metabolism; Magnesium; Metal-binding; NAD; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1..327 FT /note="dTDP-4-dehydrorhamnose reductase" FT /id="PRO_0000399900" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 264..292 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 157 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 43..45 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 44..45 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 69..70 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 69..70 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 91..93 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 91..93 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 132..133 FT /ligand="dTDP-beta-L-rhamnose" FT /ligand_id="ChEBI:CHEBI:57510" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 157 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 157 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 161 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 161 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:P26392" FT BINDING 182 FT /ligand="dTDP-beta-L-rhamnose" FT /ligand_id="ChEBI:CHEBI:57510" FT /evidence="ECO:0000250|UniProtKB:P26392" FT SITE 132 FT /note="Could provide a fine-tuning to achieve optimal pKa FT matching between active site and substrate" FT /evidence="ECO:0000250|UniProtKB:P26392" SQ SEQUENCE 327 AA; 34254 MW; 5AD5A5F7337A7276 CRC64; MDLINGMGTS PGYWRTPREP GNDHRRARLD VMAQRIVITG AGGMVGRVLA DQAAAKGHTV LALTSSQCDI TDEDAVRRFV ANGDVVINCA AYTQVDKAED EPERAHAVNA VGPGNLAKAC AAVDAGLIHI STDYVFGAVD RDTPYEVDDE TGPVNIYGRT KLAGEQAVLA AKPDAYVVRT AWVYRGGDGS DFVATMRRLA AGDGAIDVVA DQVGSPTYTG DLVGALLQIV DGGVEPGILH AANAGVASRF DQARATFEAV GADPERVRPC GSDRHPRPAP RPSYTVLSSQ RSAQAGLTPL RDWREALQDA VAAVVGATTD GPLPSTP //