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Database: UniProt
Entry: A0A014NL56_9BURK
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ID   A0A014NL56_9BURK        Unreviewed;       296 AA.
AC   A0A014NL56;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=AX13_17975 {ECO:0000313|EMBL:EXU80178.1};
OS   Comamonas aquatica DA1877.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU80178.1, ECO:0000313|Proteomes:UP000020766};
RN   [1] {ECO:0000313|EMBL:EXU80178.1, ECO:0000313|Proteomes:UP000020766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA1877 {ECO:0000313|EMBL:EXU80178.1,
RC   ECO:0000313|Proteomes:UP000020766};
RA   Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P.,
RA   Caudy A.A., Walhout A.J.;
RT   "Interspecies Systems Biology Uncovers Metabolites Affecting C. elegans
RT   Gene Expression and Life History Traits.";
RL   Submitted (JAN-2014) 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|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:EXU80178.1}.
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DR   EMBL; JBOK01000009; EXU80178.1; -; Genomic_DNA.
DR   RefSeq; WP_043383073.1; NZ_JBOK01000009.1.
DR   AlphaFoldDB; A0A014NL56; -.
DR   STRING; 225991.MA05_04500; -.
DR   PATRIC; fig|1457173.3.peg.1839; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000020766; 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   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
DR   NCBIfam; TIGR01214; rmlD; 1.
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   ECO:0000313|EMBL:EXU80178.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020766}.
FT   DOMAIN          1..295
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   296 AA;  32228 MW;  49F932EB6CDC1DE6 CRC64;
     MKILLLGCAG QVGWELQRSL AVLGEVVALD RRSTPLCGDI GQLQALAQTV RTVRPDVIVN
     AAAHTAVDRA EGEPELARLL NAAAPGVLAH EALALDALLV HYSTDYVFDG SGTAPRDEQA
     PVAPLSVYGK TKLEGEQAIQ ASGCRHLIFR TSWVYAARGG NFAKTMLRLG QERERLTVIN
     DQWGAPTGAD LLADVTAHAI RHVQRHPQDQ GLYHCVAGGA TTWHAYASEV IDQARQLRPD
     LHWPVREVAP VPTSAFPTPA RRPANSRLSS DKLQRTMGLY LPPWQQGVAR MLREIL
//
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