ID   A0A0G0I4A2_9BACT        Unreviewed;       291 AA.
AC   A0A0G0I4A2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=US68_C0008G0018 {ECO:0000313|EMBL:KKQ50133.1};
OS   Candidatus Shapirobacteria bacterium GW2011_GWE1_38_10.
OC   Bacteria; Candidatus Shapirobacteria.
OX   NCBI_TaxID=1618488 {ECO:0000313|EMBL:KKQ50133.1, ECO:0000313|Proteomes:UP000034231};
RN   [1] {ECO:0000313|EMBL:KKQ50133.1, ECO:0000313|Proteomes:UP000034231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKQ50133.1}.
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DR   EMBL; LBTX01000008; KKQ50133.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0I4A2; -.
DR   PATRIC; fig|1618488.3.peg.434; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000034231; 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   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          1..288
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   291 AA;  32471 MW;  CB3324808D579B18 CRC64;
     MKIIGTGLTG LVGSRITELN PDIEFVNISI ETGISILDPI SLEKVFTDNP DAQAVLHLAA
     FTDTNAAWDQ KGDKTGLCYQ LNVNGTQNIV NMCKKYNKYL IHISTDYVFN GQKDTPYIEE
     DAVSAVEWYG ETKAMAEKVV TDSFIPASIV RLAFPYRAKY ETKIDIIRKI KFKIENGDTL
     NLFDDQITTP TFVDDIANGL KIFFDKKPTG IYHLVGSSSQ SPYQMAMTVA EVFALDTSKI
     IATKLSDYLK TENARPFAKN AALSNEKVKT LGIQMKTLRE GLEEVKKQIN Q
//