ID   A0A1W9HAV0_9PROT        Unreviewed;       730 AA.
AC   A0A1W9HAV0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
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=A4S16_03535 {ECO:0000313|EMBL:OQW44372.1};
OS   Proteobacteria bacterium SG_bin6.
OC   Bacteria; Pseudomonadota.
OX   NCBI_TaxID=1827383 {ECO:0000313|EMBL:OQW44372.1, ECO:0000313|Proteomes:UP000192863};
RN   [1] {ECO:0000313|EMBL:OQW44372.1, ECO:0000313|Proteomes:UP000192863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG_bin6 {ECO:0000313|EMBL:OQW44372.1};
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:OQW44372.1}.
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DR   EMBL; LWDJ01000044; OQW44372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9HAV0; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000192863; 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; 3.20.20.80; 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          446..699
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   730 AA;  79500 MW;  5A692F4A5181FBC5 CRC64;
     MAPPLELWGG LECTLNRVGD RFGDQLTLSG HRDRPDDIGR IASLGLSAVR YPVLWEQVSP
     DHPEQADWAF PDARLDALRA RGLRVIAGLV HHGSGPAYTD LLDDQGFATG LARHAARVAK
     RYPWIEDWTP VNEPLTTARF AALYGHWYPH RRDERSFWRA LLNQIDGTRL AMVAIRRVIP
     HARLIQTDDL GRSFATPMLA DQAAFDNLRR WASWDLLCGM VTRQHPLWAR LVDFGFADRL
     SAIADAPCPP DIIGINHYLT SDRFLDERLH RYPPESHGGN GRQAYADVAA IRVLDPPPPG
     IAGAVREAWA RYRRPIAITE VHNGCTRDEQ LRWLAEGWDT AQALRGEGID LRAVTAWSLF
     GSCGWNTLLT APGRYEPGVF DVSGGDVRET AAADLLCGLP IDAPRPPVAR TPGWWRRPIR
     LEHRVVHLGQ PRPLAAPGTP DDVPPLLICG ATGTLGRAFA RACAARNIPY VLTDRRQLDL
     SDPESIVRAL DRHRPWAVVN AAGYVRVDAA ELERAQCFEA NCEGPARLAR AAAARGIATL
     NFSSDLVFDG AKGDAYVERD APVPLNAYGE SKARMEAALA GLAGRHLIVR TAAFFSPFDG
     HNFAAHAAHA LRSGQRFAAA EDQVMTPTFV PHLVDAALDL LIDPAEGVWH LTNGAAMSWA
     EFAYAVARAL GLDTGLIDAV PAARLGFTAP RPPAVPLAST RGALMPSFDA ALSGFAAGLA
     VQNEAPRVAA
//