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Database: UniProt
Entry: F6B9R3_DESCC
LinkDB: F6B9R3_DESCC
Original site: F6B9R3_DESCC 
ID   F6B9R3_DESCC            Unreviewed;       284 AA.
AC   F6B9R3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   OrderedLocusNames=Desca_0882 {ECO:0000313|EMBL:AEF93761.1};
OS   Desulfotomaculum nigrificans (strain DSM 14880 / VKM B-2319 / CO-1-SRB)
OS   (Desulfotomaculum carboxydivorans).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=868595 {ECO:0000313|EMBL:AEF93761.1, ECO:0000313|Proteomes:UP000009226};
RN   [1] {ECO:0000313|Proteomes:UP000009226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC   {ECO:0000313|Proteomes:UP000009226};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA   Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT   "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL   Submitted (MAY-2011) 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}.
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DR   EMBL; CP002736; AEF93761.1; -; Genomic_DNA.
DR   RefSeq; WP_003540182.1; NC_015565.1.
DR   AlphaFoldDB; F6B9R3; -.
DR   STRING; 868595.Desca_0882; -.
DR   KEGG; dca:Desca_0882; -.
DR   eggNOG; COG1091; Bacteria.
DR   HOGENOM; CLU_045518_1_2_9; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000009226; 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,
KW   ECO:0000313|EMBL:AEF93761.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009226}.
FT   DOMAIN          1..277
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   284 AA;  31287 MW;  513C2E898D8664A7 CRC64;
     MIILVTGAAG MLGQDVVAEL ARRGHRVLPM TRTELNITDL SQVRQVILSG QPDIVINCAA
     YTAVDQAEQD RERAMQINGL GVGNLALVCG ELEIPLVQIS TDYVFSGQKP GAYTVFDQPQ
     PINAYGWSKL AGEKYVLQLL QRFYLVRTSW LFGLYGNNFV ETILRLAQER KELTVVDDQH
     GCPTWTQDLA RAVADLIATG RYGVYHVTNQ GATTWFGLAS AIISQSGFDT VVKPVPTSAY
     PRPAARPVNS VLDSFPLKET IGYLLPSWQD ALARYLQLRK GGTR
//
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