ID Q47F93_DECAR Unreviewed; 320 AA.
AC Q47F93;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 85.
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 OrderedLocusNames=Daro_1741 {ECO:0000313|EMBL:AAZ46488.1};
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ46488.1};
RN [1] {ECO:0000313|EMBL:AAZ46488.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RCB {ECO:0000313|EMBL:AAZ46488.1};
RA Salinero K.K., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S.,
RA Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT "Complete sequence of Dechloromonas aromatica RCB.";
RL Submitted (AUG-2005) 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}.
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DR EMBL; CP000089; AAZ46488.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47F93; -.
DR STRING; 159087.Daro_1741; -.
DR KEGG; dar:Daro_1741; -.
DR eggNOG; COG1091; Bacteria.
DR HOGENOM; CLU_045518_1_0_4; -.
DR UniPathway; UPA00124; -.
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:AAZ46488.1}.
FT DOMAIN 18..312
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 320 AA; 34596 MW; C865BDA068E3C84D CRC64;
MPREMAYSTG FQLACIAMKI LLLGKDGQVG WQLQRSLAPH GDVVACGRAQ CDLSDLAQIR
SVVRETRPSV IVNATAYTAV DKAESEPELA RRINADAPGV LAEEAAQLNA LLVHYSTDYV
YDGAKASAYL ETDVTAPQSV YGRTKLAGEE AIRAAGGKSL IFRTSWVFGA RGGNFVKTIL
RLAREKESLN VVADQIGSPT PAALIATVTG IALAMLQHGK LLEKSESRLY HLAASRPVSW
CDFARTIVGL AGQAPGFDLR LKSGAIQAIS TAEYPTPACR PANSRLDCGR LENDFGLQMP
DWQPYLERML QLLALKQNGY
//
