ID   G3GGS0_STREE            Unreviewed;       284 AA.
AC   G3GGS0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
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:AEO88721.1};
OS   Streptococcus pneumoniae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313 {ECO:0000313|EMBL:AEO88721.1};
RN   [1] {ECO:0000313|EMBL:AEO88721.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Elberse K.E., Witteveen S., van der Heide H., van de Pol I., Schot C.,
RA   van der Ende A., Berbers G., Schouls L.;
RT   "Sequence Diversity within the Capsular Genes of Streptococcus pneumoniae
RT   Serogroup 6 and 19.";
RL   PLoS ONE 6:e25018-e25018(2011).
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; JF911512; AEO88647.1; -; Genomic_DNA.
DR   EMBL; JF911513; AEO88662.1; -; Genomic_DNA.
DR   EMBL; JF911514; AEO88677.1; -; Genomic_DNA.
DR   EMBL; JF911516; AEO88706.1; -; Genomic_DNA.
DR   EMBL; JF911517; AEO88721.1; -; Genomic_DNA.
DR   EMBL; JF911518; AEO88736.1; -; Genomic_DNA.
DR   EMBL; JF911519; AEO88751.1; -; Genomic_DNA.
DR   EMBL; JF911521; AEO88781.1; -; Genomic_DNA.
DR   RefSeq; WP_000600921.1; NZ_UHGC01000001.1.
DR   PATRIC; fig|1313.5281.peg.16; -.
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..280
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   284 AA;  32230 MW;  77268991B5C1F9D9 CRC64;
     MILITGANGQ LGTELRYLLD ERNVDYVAVD VTEMDITNSE MVEKVFAEVK PTLVYHCAAY
     TAVDAAEDEG KELDFAINVT GTENVAKASE KYGAILVYIS TDYVFDGKKP VGQEWEVDDI
     PDPQTEYGRT KRMGEELVEN LTSQHYIIRT AWVFGNYGKN FVFTMQSLAK THKTLTVVND
     QYGRPTWTRT LAEFMTYVTE NQKEYGYYHL SNDAAEDTTW YDFASEILKD SDVEVVPVDS
     SKFPAKAKRP LNSTMSLAKA KATGFVIPTW QDALKEFYKQ EVRK
//