ID   A0A1M6T0F4_9FIRM        Unreviewed;       282 AA.
AC   A0A1M6T0F4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=SAMN02745243_03087 {ECO:0000313|EMBL:SHK50390.1};
OS   Hespellia stercorisuis DSM 15480.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Hespellia.
OX   NCBI_TaxID=1121950 {ECO:0000313|EMBL:SHK50390.1, ECO:0000313|Proteomes:UP000184301};
RN   [1] {ECO:0000313|EMBL:SHK50390.1, ECO:0000313|Proteomes:UP000184301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15480 {ECO:0000313|EMBL:SHK50390.1,
RC   ECO:0000313|Proteomes:UP000184301};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FQZY01000054; SHK50390.1; -; Genomic_DNA.
DR   RefSeq; WP_073112061.1; NZ_FQZY01000054.1.
DR   AlphaFoldDB; A0A1M6T0F4; -.
DR   STRING; 1121950.SAMN02745243_03087; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000184301; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184301}.
FT   DOMAIN          3..279
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   282 AA;  31509 MW;  D73E13D77286BAE9 CRC64;
     MLKVWINGAN GQLGTALNAV VDPLEFEIFN TDKAELDITD LDEVISFGKI NRPDIIINCA
     ALTNVDVCEE NPGAAYNVNA LGARNLSIIA GDLNAKLVQI STDDVFDGRS SEPYNEFDKT
     SPHTVYGRSK LAAENYVKEF TNKHFIIRSN WVYGRGNNFV REFLKMAKAE IPISIASDQF
     GSPTSARELA RFILYLIQGN EYGTYHATCR GVCSRYAFAK EILRLTGYKT RIKAVPATEA
     HLSSIRPAYA VLDNFIINIK GEYQMPQWED ALAAYLKNME EK
//