ID   Q6L5P6_STRMT            Unreviewed;       281 AA.
AC   Q6L5P6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   13-SEP-2023, entry version 57.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   Name=rmlD {ECO:0000313|EMBL:BAD22652.1};
OS   Streptococcus mitis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=28037 {ECO:0000313|EMBL:BAD22652.1};
RN   [1] {ECO:0000313|EMBL:BAD22652.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16164562; DOI=10.1111/j.1365-2958.2005.04820.x;
RA   Yoshida Y., Ganguly S., Bush C.A., Cisar J.O.;
RT   "Carbohydrate engineering of the recognition motifs in streptococcal co-
RT   aggregation receptor polysaccharides.";
RL   Mol. Microbiol. 58:244-256(2005).
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; AB181235; BAD22652.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6L5P6; -.
DR   UniPathway; UPA00124; -.
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   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   3: Inferred from homology;
KW   NADP {ECO:0000256|RuleBase:RU364082};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364082}.
FT   DOMAIN          2..267
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   281 AA;  31696 MW;  0AD4AFC31034590B CRC64;
     MILITGANGQ LGTELRYLLD ERNVNYVAVD VAEMDITNAE MVEKVFAEVK PTLVYHCAAY
     TAVDAAEDEG KELDFAINVT GTENVAKASE KYGATLVYIS TDYVFDGKKP VGQEWEVDDL
     PDPQTEYGRT KRMGEELVEN LTSQHYIIRT AWVFGNYGKN FVFTMKNLAK THKTLTVVND
     QHGRPTWTRT LAEFMTYLTE NQKEFGYYHL SNDSTEDTTW YDFAVEILKD SDVEVVPVDS
     SKFPAKAKRP LNSTMSLAKA KATGSSFQLG KMHLKSFINK K
//