ID A0A0G1I3V1_9BACT Unreviewed; 389 AA.
AC A0A0G1I3V1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=UW11_C0009G0013 {ECO:0000313|EMBL:KKT26557.1};
OS Parcubacteria group bacterium GW2011_GWA2_43_9b.
OC Bacteria.
OX NCBI_TaxID=1618828 {ECO:0000313|EMBL:KKT26557.1, ECO:0000313|Proteomes:UP000034814};
RN [1] {ECO:0000313|EMBL:KKT26557.1, ECO:0000313|Proteomes:UP000034814}
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:KKT26557.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCHB01000009; KKT26557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1I3V1; -.
DR STRING; 1618828.UW11_C0009G0013; -.
DR PATRIC; fig|1618828.3.peg.340; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000034814; 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; 3.
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 3..102
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT DOMAIN 126..242
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT DOMAIN 269..386
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT REGION 332..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 43294 MW; 7632B312C7D27298 CRC64;
MKKVLIIGVK GMLGQELVRV FSADADYEVF GWDKLLMSDI NTIDITDEAQ VRDKVLKLSP
AIIINAAAYN DVDRCEEPAE FALAKKLNGL APGYLAKAAR EIHNPPTPLC VRGAGDGDSL
RRGGDDGAIF VHYSTDYVFD GQKEGGYKEN DEPFPIQNYG ISKLMGEQEV QKAGGQYYII
RLQKLFGWPA QSTSAKKSFF ETMLFLARTK KKLEIVDEEL ANFTYAPDLA ERTKWLVEIS
DSNTEQVRGF GRGLEKSSLT PLLQSGEPYP FGIYHIINEG APMTWFGAAK VLFEMAQQRH
PEPSAGGEGY LTNARPASAG DFSLRSRSVQ NDKKENLHND SIPQLTPVSS SKFSRPAKRP
KYSILLNTKL PPLRPWPEAL KEFLADRPL
//
