ID   A0A0J1BKW1_9SPHI        Unreviewed;       304 AA.
AC   A0A0J1BKW1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, 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=AB669_07195 {ECO:0000313|EMBL:KLT65958.1};
OS   Pedobacter sp. BMA.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT65958.1, ECO:0000313|Proteomes:UP000036014};
RN   [1] {ECO:0000313|EMBL:KLT65958.1, ECO:0000313|Proteomes:UP000036014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BMA {ECO:0000313|EMBL:KLT65958.1,
RC   ECO:0000313|Proteomes:UP000036014};
RA   Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT   "Pedobacter sp. BMA.";
RL   Submitted (JUN-2015) 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:KLT65958.1}.
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DR   EMBL; LECU01000004; KLT65958.1; -; Genomic_DNA.
DR   RefSeq; WP_047798628.1; NZ_LECU01000004.1.
DR   AlphaFoldDB; A0A0J1BKW1; -.
DR   STRING; 1663685.AB669_07195; -.
DR   PATRIC; fig|1663685.3.peg.1511; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000036014; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036014}.
FT   DOMAIN          3..294
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   304 AA;  33518 MW;  4F62C8A70065C870 CRC64;
     MKTILVTGSN GLLGQKITEK VIAGGRVKLV ATSKGKNRFP SSSGYQYAEM DILNPEQVKD
     VITLYQPDAI IHTAAMTNVD TAQANQESCY QLNVVAVNTL ISVCEANNIQ LIHLSTDFVF
     DGDAGPYKEN DQVNPLSYYG ESKVLAEQAL KKSNIHWTII RTILVYGITN DMSRSNIVLW
     AKGALEKRLP VNVVNDQWRM PTLAEDLAEA CLLAAEQSAG GVYHISGKDY MSIADIVRKV
     ADYWTLDHSI VTEVSSQTLN QSATRPMRTG FVLDKAVADL GYSPHSFEEG LKMLDDQMKG
     RQQV
//