ID   A0A2D6FIV4_9BACT        Unreviewed;       297 AA.
AC   A0A2D6FIV4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   03-MAY-2023, entry version 10.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=CMI54_00305 {ECO:0000313|EMBL:MAF42595.1};
OS   Parcubacteria group bacterium.
OC   Bacteria.
OX   NCBI_TaxID=2026774 {ECO:0000313|EMBL:MAF42595.1, ECO:0000313|Proteomes:UP000221304};
RN   [1] {ECO:0000313|Proteomes:UP000221304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MAF42595.1}.
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DR   EMBL; NYZL01000003; MAF42595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D6FIV4; -.
DR   Proteomes; UP000221304; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
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..284
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   297 AA;  33660 MW;  0058DD25B885A3B5 CRC64;
     MILVLGQTGY IGTQFINELN NRNLSYEGIS RVNINYCNFS DLYSYLTTGS CLGPARYDLI
     INCAGYVGKP NVDACEDHKA ETIEGNVVLP KTISNVCREA GVKFMHISSG CIYDGYDKEF
     TEEDPPNFSF KQNNCSFYSG SKALAEDLID KDNSYICRLR IPFDEFDNSR NYISKLKNYD
     KLLNVKNSIS HRGDFVKACL DLYLNNCPTG IYNIVNSGHV TTEQVARLMS KYNIRNDFNF
     FSNEKTFYEF GAKAPRSNCL LDNSKLSLVG VQIRDVNEAL EEALFNWVYK EGNSPIE
//