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Database: UniProt
Entry: F8F741_PAEMK
LinkDB: F8F741_PAEMK
Original site: F8F741_PAEMK 
ID   F8F741_PAEMK            Unreviewed;       309 AA.
AC   F8F741;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   OrderedLocusNames=KNP414_06545 {ECO:0000313|EMBL:AEI45066.1};
OS   Paenibacillus mucilaginosus (strain KNP414).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1036673 {ECO:0000313|EMBL:AEI45066.1, ECO:0000313|Proteomes:UP000006620};
RN   [1] {ECO:0000313|Proteomes:UP000006620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNP414 {ECO:0000313|Proteomes:UP000006620};
RA   Wang J., Hu S., Hu X., Zhang B., Dong D., Zhang S., Zhao K., Wu D.;
RT   "Complete genome sequence of Paenibacillus mucilaginosus KNP414.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEI45066.1, ECO:0000313|Proteomes:UP000006620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNP414 {ECO:0000313|EMBL:AEI45066.1,
RC   ECO:0000313|Proteomes:UP000006620};
RX   PubMed=24158556;
RA   Lu J.J., Wang J.F., Hu X.F.;
RT   "Genome Sequence of Growth-Improving Paenibacillus mucilaginosus Strain
RT   KNP414.";
RL   Genome Announc. 1:e00881-13(2013).
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; CP002869; AEI45066.1; -; Genomic_DNA.
DR   RefSeq; WP_013920210.1; NC_015690.1.
DR   AlphaFoldDB; F8F741; -.
DR   KEGG; pms:KNP414_06545; -.
DR   PATRIC; fig|1036673.3.peg.6101; -.
DR   HOGENOM; CLU_045518_1_2_9; -.
DR   OMA; AGETTWH; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000006620; 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          1..278
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
FT   REGION          285..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   309 AA;  34056 MW;  672B503ED2C87747 CRC64;
     MKIGITGAGG QLGQDLIRML ESRHELVAWK HQDLNITDEK AVEQAFALHR PDAVIHAAAF
     TGVDAAEKNL DAAYMVNAFG TRHVAWAAHT IGAKMVYVST DYVFDGRKGE PYTEGDRTAP
     LGIYGNSKLL GEKFTEFLCD RHFIVRTSWL YGLSGSNFVT KVLQLAKEQG SLRMVSDQYG
     SPTYTLDLAA QIAELIETEE YGVYHVSNRG FCSRLRFAEA ILEIAGLAGV RLEAVESAEL
     SLPAERPVHS ALSDLALRRR GFGRMRHWKS ALEAFIREDL KCGGLEHNED GEEGPKDDSK
     RADQDAGPA
//
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