ID A0A1I6RNR9_9BACL Unreviewed; 304 AA.
AC A0A1I6RNR9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=SAMN05444972_105244 {ECO:0000313|EMBL:SFS66349.1};
OS Marininema halotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Marininema.
OX NCBI_TaxID=1155944 {ECO:0000313|EMBL:SFS66349.1, ECO:0000313|Proteomes:UP000198660};
RN [1] {ECO:0000313|EMBL:SFS66349.1, ECO:0000313|Proteomes:UP000198660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45789 {ECO:0000313|EMBL:SFS66349.1,
RC ECO:0000313|Proteomes:UP000198660};
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; FPAA01000005; SFS66349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6RNR9; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000198660; 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 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 1..235
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 304 AA; 34519 MW; B7E726B864301361 CRC64;
MKILVIGANG MAGHMIQDYL IQHTSYEIWA TSRSEKSTHR RLFLDALDTN RLSGLLLTLK
PDLVINAIGL LNQDAENHPQ WADQINGELP QLLSNYGIAL GFKLIHISTD CVFSGASGDY
RESDTRDASG VYPESKKRGE NIDPRHLLIR TSIIGPELRK GIGLFHWYMN QRKPVQGFRN
VWWNGVTTLE LAKCIHWAIE HPLSGLVHLC VRKKISKHDL LLTIQDIFPG NRAPIQPNNA
PCSNKSLVNT RCDFPYVPPD YQTMLVNLRE WMELAPPSRY AQYDWVRTSP SHPSIPTPKK
KLDP
//
