ID A0A0G1R560_9BACT Unreviewed; 302 AA.
AC A0A0G1R560;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=UX72_C0006G0026 {ECO:0000313|EMBL:KKU52349.1};
OS Parcubacteria group bacterium GW2011_GWA2_47_10.
OC Bacteria.
OX NCBI_TaxID=1618839 {ECO:0000313|EMBL:KKU52349.1, ECO:0000313|Proteomes:UP000034777};
RN [1] {ECO:0000313|EMBL:KKU52349.1, ECO:0000313|Proteomes:UP000034777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKU52349.1}.
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DR EMBL; LCNG01000006; KKU52349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1R560; -.
DR PATRIC; fig|1618839.3.peg.523; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000034777; 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 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}.
FT DOMAIN 8..298
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 302 AA; 34567 MW; F61D1AC3236C7562 CRC64;
MKKKQKKKVL IFGAGGMLGK ECKRQLSNSA MWYVIGLSER DIDITNYDSL FCAIKKIRPD
VVINCAALIN IDDCEKDPLR AWMVNAIGPG YIVRALKEAG RRRTVFVHIS TSDVFGGRKP
RWKEKNIPSP VNAYGWSKLY GEKNIEHEAR GSGIRYYIIR TSWLYSEYRP TFIDLVISAL
RKKKQIPLVT DQRSVPTSAR ELAAEIEKIL LNRNKPGIYH VINHSTGGVS KYQIGTEILR
IMNASSHSSG RRFSRYYLTK SSKKDMFKVA RPASPVLINT KLPQMRDWRS SLGEYIRRHV
KS
//
