ID   A0A1W9H894_9PROT        Unreviewed;       727 AA.
AC   A0A1W9H894;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   03-MAY-2023, entry version 14.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|ARBA:ARBA00017099, ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|ARBA:ARBA00012929, ECO:0000256|RuleBase:RU364082};
GN   ORFNames=A4S12_04610 {ECO:0000313|EMBL:OQW43658.1};
OS   Proteobacteria bacterium SG_bin5.
OC   Bacteria; Pseudomonadota.
OX   NCBI_TaxID=1827382 {ECO:0000313|EMBL:OQW43658.1, ECO:0000313|Proteomes:UP000192868};
RN   [1] {ECO:0000313|EMBL:OQW43658.1, ECO:0000313|Proteomes:UP000192868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG_bin5 {ECO:0000313|EMBL:OQW43658.1};
RX   PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA   Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT   "Comammox in drinking water systems.";
RL   Water Res. 116:332-341(2017).
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|ARBA:ARBA00000079,
CC         ECO:0000256|RuleBase:RU364082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364082};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|RuleBase:RU364082};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004781, 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:OQW43658.1}.
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; LWDI01000032; OQW43658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9H894; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000192868; 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; 3.20.20.80; Glycosidases; 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; IPR017853; Glycoside_hydrolase_SF.
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; SSF51445; (Trans)glycosidases; 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          445..699
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   727 AA;  77974 MW;  4616AA698E33282C CRC64;
     MAQPLELWGG LECTLNRVGD GFTDQFALSG HRARPGDIDR IAGLGLKALR YPVLWEQVSP
     DHPDQTDWAF SDERLGALRA RGIRVIAGLV HHGSGPAYTD LLDDAAFATG LARHAARVAA
     RYPWIEDWTP VNEPLTTARF SALYGLWYPH RRDAGDCWRA LLNQIDAVRL AMAAIRAVIP
     GARLIQTDDL GQCHATPELA EQARFENLRR WASWDLLCGQ VTEAHPLWAE IARFGLAHRL
     AAIAAAPCPP DVIGINHYLT SDRFLDHRLQ RYPAESHGGN GRQAYADVAA IRVLDPAPPG
     FEGAVRAAWA RYRRPIALTE VHNGCTRDEQ LRWLADAWDA GQRLRGEGVD LRAITAWSLF
     GSHGWDRLLT APGRYEPGVF DASGAEVRET AAAALLRALP NEATRHPLAR TLGWWRRPLR
     LLHPVVHHRG QAAPARGPGD AVPPLLICGA SGTLGQAFAR ACAARNIPYL LTARDALDLG
     CAARIEQALD RHRPWAVVNA AGYVRVDDAE HDRAACFAAN AEGAARLARA AGARGIATLS
     FSSDLVFDGA KGAPYVEADA PGPLNVYGAS KARMEAALGG LPGRQLIVRT AAFFSPFDAH
     NFAVAVARAL AAGQRFAAAA DLVVTPTYVP HLVEAALDLL IDPAEGVWHV TNGAPLSWAD
     FAHRIAEALA LDARLIDAVP AATLGFAAPR PPAVPLASTR GALMPSFEAA LAAFAAGMAG
     QEARAAA
//