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Entry: A0A1W6YSM4_9BORD
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ID   A0A1W6YSM4_9BORD        Unreviewed;       305 AA.
AC   A0A1W6YSM4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|ARBA:ARBA00017099, ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|ARBA:ARBA00012929, ECO:0000256|RuleBase:RU364082};
GN   ORFNames=CAL12_27005 {ECO:0000313|EMBL:ARP84105.1};
OS   Bordetella genomosp. 8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1416806 {ECO:0000313|EMBL:ARP84105.1, ECO:0000313|Proteomes:UP000194151};
RN   [1] {ECO:0000313|EMBL:ARP84105.1, ECO:0000313|Proteomes:UP000194151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU19157 {ECO:0000313|EMBL:ARP84105.1,
RC   ECO:0000313|Proteomes:UP000194151};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-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|ARBA:ARBA00000079,
CC         ECO:0000256|RuleBase:RU364082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364082};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|RuleBase:RU364082};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004781, 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; CP021108; ARP84105.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6YSM4; -.
DR   STRING; 1416806.CAL12_27005; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000194151; 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..300
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   305 AA;  32500 MW;  5AF8530AA39676EF CRC64;
     MKILLLGKNG QVGWELQRAL APLGELVALG REAMDAEGHT LRGDLADLDG LARTVRAVRP
     DVIVNAAAYT AVDKAESDVE QAELLNGLAP GVLAREAAAM GALLIHYSTD YVFDGSGARP
     WTETDATGPV SVYGRTKLQG EQAIAAAGCR HLIFRTSWVY AARGGNFAKT MLRLAGERDA
     LSVIDDQKGA PTGADLIADV TAHAMVRALR EPALCGLYHL VAAGETSWNE YARLVLSVAL
     KRGFELKATP DKVAPVPTSS YKTAARRPLN SRLDTAKLRG AFGVSLPAWQ SGVERMIAEI
     SENKP
//
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