ID A0A1I5LBY5_9PSEU Unreviewed; 307 AA.
AC A0A1I5LBY5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=SAMN05421805_1309 {ECO:0000313|EMBL:SFO94366.1};
OS Saccharopolyspora antimicrobica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=455193 {ECO:0000313|EMBL:SFO94366.1, ECO:0000313|Proteomes:UP000199398};
RN [1] {ECO:0000313|EMBL:SFO94366.1, ECO:0000313|Proteomes:UP000199398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFO94366.1,
RC ECO:0000313|Proteomes:UP000199398};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|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}.
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DR EMBL; FOUP01000030; SFO94366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5LBY5; -.
DR STRING; 455193.SAMN05421805_1309; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000199398; 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 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}.
FT DOMAIN 6..296
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 307 AA; 32801 MW; 32ABFE60F36EA84C CRC64;
MSRLAVLVPG GRGQVGSELA RIVSARSGAL VHAPGSGELD ITDHEAVADA VDSFAETARD
ADLRPVVVNA SAYTAVDAAE SDPERAALVN AEGPAQLAKA CHRSGIPLLH LSTDYVFGGD
ADRPYEPADE PAPRTVYGRT KLDGERAVLD SGARAWVVRT AWVYGARGGN FVKTMARLSR
ERDSLSVVAD QIGSPTWAAD LAQGLLELAE RVAERRGPDR KVLHCTNSGQ VSWCDFARAI
FTELGLDESR VQPCTTADFP RPAPRPAYSV LSDAAWREAG LTPLRSWREA LRAAFETDGE
VLRGEAG
//
