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Database: UniProt
Entry: A0A2A9DUR7_9MICO
LinkDB: A0A2A9DUR7_9MICO
Original site: A0A2A9DUR7_9MICO 
ID   A0A2A9DUR7_9MICO        Unreviewed;       311 AA.
AC   A0A2A9DUR7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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=ATJ78_1357 {ECO:0000313|EMBL:PFG30428.1};
OS   Microbacterium agarici.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=630514 {ECO:0000313|EMBL:PFG30428.1, ECO:0000313|Proteomes:UP000221369};
RN   [1] {ECO:0000313|EMBL:PFG30428.1, ECO:0000313|Proteomes:UP000221369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21798 {ECO:0000313|EMBL:PFG30428.1,
RC   ECO:0000313|Proteomes:UP000221369};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2017) 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}.
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:PFG30428.1}.
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DR   EMBL; PDJE01000001; PFG30428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9DUR7; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000221369; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000221369}.
FT   DOMAIN          17..291
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   311 AA;  33860 MW;  E0FDBA49F2F0BFAD CRC64;
     MGPKTEMYSQ LGEGAVMRIL VTGARGMLGT DLREQLIHHE VTAADHEYLD IADAAAVRRA
     VAGHDVVINA AAYTSVDEAE KNEDLAYRIN ADGPRYLAEA AKAGGARFLQ VSTDYVFDGT
     SPLPYSENAP LHPVSAYGRT KAAGERFVRS IYPDGTFIVR TAWLYGRNGS NFAGTMLTLA
     SSRQTIDVVS DQRGQPTWTR DLAVQIQRLL DCNAAPGIYH GTNSGDATWF DFAQAVFAEC
     GLDPSRIRAT DSASFAQSAR RPANSVLGHA AWRATPLPAM RPWRDALHDA ARTGVFEHLL
     TTRRSTMTDL E
//
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