ID   M8DIZ5_9BACL            Unreviewed;       305 AA.
AC   M8DIZ5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=I532_05325 {ECO:0000313|EMBL:EMT53407.1};
OS   Brevibacillus borstelensis AK1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT53407.1, ECO:0000313|Proteomes:UP000012081};
RN   [1] {ECO:0000313|EMBL:EMT53407.1, ECO:0000313|Proteomes:UP000012081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK1 {ECO:0000313|EMBL:EMT53407.1,
RC   ECO:0000313|Proteomes:UP000012081};
RA   Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA   Sivakumar N.;
RT   "Assembly of a new bacterial strain Brevibacillus borstelensis AK1.";
RL   Submitted (MAR-2013) 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:EMT53407.1}.
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DR   EMBL; APBN01000002; EMT53407.1; -; Genomic_DNA.
DR   AlphaFoldDB; M8DIZ5; -.
DR   STRING; 1300222.I532_05325; -.
DR   PATRIC; fig|1300222.3.peg.1090; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000012081; 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:UP000012081}.
FT   DOMAIN          25..303
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   305 AA;  34250 MW;  FBC185BA6058AF4E CRC64;
     MVQKQALIMD MRLKTRVSGN RVGSMKILVT GANGQLGREL VKVLSAHHQV IGCTRNELDV
     TDLSKARDIV QEARPEIVVH TAAYTHVDQA EADQDRAFLV NAYGTRNMTV AAQQAGAKMM
     YISTDYVFDG RSTKPYREYD FVNPVNVYGK SKLAGEDMVK TLSDKYFIVR TSWVYGRHGS
     NFVKNMLRLA ETRTEIDVVC DQVGSPTYAP ELAWFIKELL ESEKYGIYHV SNTGACSRYE
     WAKAIFAAAG LGVTVRPVDT AKFLLPAARP AYSVLDYMAI RLNGFSTLRH WRTALTQFID
     ELRSI
//