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Database: UniProt
Entry: R0BS70_9FIRM
LinkDB: R0BS70_9FIRM
Original site: R0BS70_9FIRM 
ID   R0BS70_9FIRM            Unreviewed;       294 AA.
AC   R0BS70;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=HMPREF1085_01683 {ECO:0000313|EMBL:ENZ51488.1};
OS   Enterocloster bolteae 90A9.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Enterocloster.
OX   NCBI_TaxID=997894 {ECO:0000313|EMBL:ENZ51488.1, ECO:0000313|Proteomes:UP000013126};
RN   [1] {ECO:0000313|EMBL:ENZ51488.1, ECO:0000313|Proteomes:UP000013126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90A9 {ECO:0000313|EMBL:ENZ51488.1,
RC   ECO:0000313|Proteomes:UP000013126};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium bolteae 90A9.";
RL   Submitted (JAN-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:ENZ51488.1}.
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DR   EMBL; AGYH01000004; ENZ51488.1; -; Genomic_DNA.
DR   RefSeq; WP_002575012.1; NZ_KB851182.1.
DR   AlphaFoldDB; R0BS70; -.
DR   PATRIC; fig|997894.4.peg.1785; -.
DR   HOGENOM; CLU_045518_2_1_9; -.
DR   OrthoDB; 9808602at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000013126; 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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
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          4..274
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
FT   REGION          110..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   294 AA;  33109 MW;  86376BFF8DC54418 CRC64;
     MNRRLLITGA GGFLGSRICE YYSNRDGYEA VGVTHRELDI EDFVAVSAFI KAIRPDYVLH
     CAAISNTGTC ERNPVLSEKV NVRGTINLAK ACRNAGSRMI FTSSDQIYNT SHSMEPNREG
     SEGKPGNVYG RDKKRAEEAM LTYLPDAVAL RLTWMYDAPS RGRAAGQGLL QKLADALKER
     REVEFPVHDY RGITYVWEVV RHLEEAMGLP GGVYNFGSEN RYNTFDTARL FLRELAGSDS
     AGILKRNDER FASCPRNLTM DTDKIKSYGI RFFNTSEGIR KCSMEHREMS QARC
//
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