ID A0A0G0PAI6_9BACT Unreviewed; 344 AA.
AC A0A0G0PAI6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, 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=UT50_C0001G0013 {ECO:0000313|EMBL:KKR22101.1};
OS Candidatus Moranbacteria bacterium GW2011_GWA2_39_41.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618695 {ECO:0000313|EMBL:KKR22101.1, ECO:0000313|Proteomes:UP000034867};
RN [1] {ECO:0000313|EMBL:KKR22101.1, ECO:0000313|Proteomes:UP000034867}
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:KKR22101.1}.
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DR EMBL; LBXA01000001; KKR22101.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0PAI6; -.
DR PATRIC; fig|1618695.3.peg.13; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000034867; 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 19..342
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 344 AA; 38699 MW; 2AD39C13F342B528 CRC64;
MIKNIKNKVE KIEVFGKKKV LIIGANGMLG QELVNVFKKD SDYEVVAWDR GDIDITSEKQ
VESKVTKLKP AIIINATGYN AVDKCEEDKK EYEMAKKLNG KAPGYLAKVA KKLKAVFVNY
SSDYVFDGQP EIPEPEGCSH RCSACSLHEN FVPQIGFDEE AKTHPISNYG KSKVLGEKEV
MKNTKAYYII RPSKIFGEPA KAENAKRSFF DVMLEVGKKN KEVYPVKSSS AGRPKAEFNG
VKAVDEETSC FTYAPDLAKK TKEIIEAEKP FGIYHVVNGD PCTWYEAVLE LYKQAKLKTK
VIPVLGSEFP RPAKRPHYSV LLNTKLNPMR SYKDALKEYL KSSK
//