ID   D7GXD4_9BACT            Unreviewed;       278 AA.
AC   D7GXD4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=mtbajb2F00010 {ECO:0000313|EMBL:CBL42924.1};
OS   Candidatus Magnetobacterium bavaricum.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Magnetobacterium.
OX   NCBI_TaxID=29290 {ECO:0000313|EMBL:CBL42924.1};
RN   [1] {ECO:0000313|EMBL:CBL42924.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Jogler C., Niebler M., Lin W., Kube M., Wanner G., Kolinko S., Stief P.,
RA   Beck A.J., de Beer D., Petersen N., Pan Y., Amann R., Reinhardt R.,
RA   Schuler D.;
RT   "Cultivation-independent characterization of 'Candidatus Magnetobacterium
RT   bavaricum' via ultrastructural, geochemical, ecological and metagenomic
RT   methods.";
RL   Environ. Microbiol. 12:2466-2478(2010).
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; FP929063; CBL42924.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7GXD4; -.
DR   UniPathway; UPA00124; -.
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          5..268
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   278 AA;  30877 MW;  95C7F6BE10E946E7 CRC64;
     MLAGDLIPIL AQYHYLYSQN RADLDITDAG RVFKVVDVYR PDVVVNCAAY TAVDRAETER
     EMAMLVNGIG VQNLALACSK YDVPLCHIST DYVFDGSKGA PYTPFDNTSP VNFYGESKLA
     GECYVRWLTG KFYIIRTSWL YGARGGNFVK TMLRLSTQRD EVRVVHDQVG NPTSTVSLAR
     AIKVIIESGR YGVYHVTDQT DGKLNWYDFA CEIMRLAGAG TRVVPITTAE YPTAARRPVY
     SVLDLEPSRL SVDYPLKSWD AALAECIEGI LKEGGLKV
//