ID A0A0G0ZME3_9BACT Unreviewed; 315 AA.
AC A0A0G0ZME3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=UU78_C0001G0011 {ECO:0000313|EMBL:KKS23206.1};
OS Candidatus Roizmanbacteria bacterium GW2011_GWC2_41_7.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1618487 {ECO:0000313|EMBL:KKS23206.1, ECO:0000313|Proteomes:UP000034371};
RN [1] {ECO:0000313|EMBL:KKS23206.1, ECO:0000313|Proteomes:UP000034371}
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:KKS23206.1}.
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DR EMBL; LCBY01000001; KKS23206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0ZME3; -.
DR PATRIC; fig|1618487.3.peg.11; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000034371; 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; 2.
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; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082}.
FT DOMAIN 1..77
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT DOMAIN 105..314
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 315 AA; 35692 MW; 2654DAFEE136CE29 CRC64;
MTILGTGLSG MIGSCIQETL HNTYSFEDLS TESGVDIRNF DQVLDRVKKS SSAVVLHLAA
KTDVDGCEKD RIKDSKILRS LSKPDLALRD KDPMDFDIDW KEWKNENTAY AVNVVGTLNI
VRACKEANRR LIYISTDFVF DGRENKTYSE DDKPNPINYY AQTKWWGEQV VRNLLTNYVI
VRFAYPYGTH HAVKKDFVRI IRSRLESGEE VAGITDQIIT PSFAPDIAYA LDHLIGHAVS
NQTFHLVGSD SLSPYDIAVA IADQFGYDTQ VIKKTTVEEF YKNRASRPQF LTVSNEKIRK
RGVDMKTFRE GLASL
//