ID A0A2S1ZAL4_9ACTN Unreviewed; 288 AA.
AC A0A2S1ZAL4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN Name=rfbD {ECO:0000313|EMBL:AWK12958.1};
GN ORFNames=DDQ41_16765 {ECO:0000313|EMBL:AWK12958.1};
OS Streptomyces spongiicola.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1690221 {ECO:0000313|EMBL:AWK12958.1, ECO:0000313|Proteomes:UP000245051};
RN [1] {ECO:0000313|EMBL:AWK12958.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HNM0071 {ECO:0000313|EMBL:AWK12958.1};
RA Zhou S., Huang X.;
RT "Complete genome sequence of the Type Strain of Streptomyces spongiicola
RT HNM0071, the producer of staurosporine.";
RL Submitted (MAY-2018) 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; CP029254; AWK12958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1ZAL4; -.
DR KEGG; sspo:DDQ41_16765; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000245051; Chromosome.
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 2..272
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 288 AA; 30029 MW; E7BC23AF227B3FE8 CRC64;
MLGRDMLAEL AADPEAKATG LTRGELDIAD RVAVHAAAAG HHVVVNCAAW TDVDAAEHAE
EAATAVNGTG VRHLARACAG SGSVLLHVST DYVFSGDAGH PYPEGAPTAP VNAYGRSKLA
GERAVAELLP GTGYTVRTAW LYGAHGRNFV RTMLELACRR QTLDVVADQH GQPTWSRALA
RQLAALGRAA LTGRAPAGVY HGTAAGRTTW YGLAHETFRL SGLDPERIRP VGAAAFPRPA
PRPAFGVLGH DGWSRAGVPS QLRWDDQLST ALGTPGFAEL AAAARAVG
//