ID   A0A0S7ZFM6_9BACT        Unreviewed;       289 AA.
AC   A0A0S7ZFM6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=AMJ57_01375 {ECO:0000313|EMBL:KPJ85886.1};
OS   Parcubacteria bacterium SG8_24.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1703768 {ECO:0000313|EMBL:KPJ85886.1, ECO:0000313|Proteomes:UP000051503};
RN   [1] {ECO:0000313|EMBL:KPJ85886.1, ECO:0000313|Proteomes:UP000051503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_24 {ECO:0000313|EMBL:KPJ85886.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPJ85886.1}.
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DR   EMBL; LJNP01000007; KPJ85886.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7ZFM6; -.
DR   STRING; 1703768.AMJ57_01375; -.
DR   PATRIC; fig|1703768.3.peg.1143; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000051503; 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}.
FT   DOMAIN          1..267
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   289 AA;  31143 MW;  20533932DF50E7CE CRC64;
     MKALILGAKG NLGQDLVRRF TTAGHEAVGL DRKELDVTDS AAVRQQVLAG GYDAVVNAVA
     WNDVDGAEDP ANLDRVLELN AAVPGVIAAA AAKAGAAFVH YSTDYVFDGS RPGGYREDDE
     PRPLSVYGRS KLEGERVALA AGGRVYVCRT SKLYGTPGLS TLSKPSFVHL MLKLAATKPE
     LSIVDEEVGM PTFTEDLAGA TVRLLEEGHA PGIYHLVNEG EGVTWYGFAE EIFRLQDITV
     PRRAVPSSAF PTKAERPKYA KLLNTKFPPL RDRIEALEDF LCRATVGQT
//