GenomeNet

Database: UniProt
Entry: Q07GH2_ROSDO
LinkDB: Q07GH2_ROSDO
Original site: Q07GH2_ROSDO 
ID   Q07GH2_ROSDO            Unreviewed;       307 AA.
AC   Q07GH2;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 86.
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   Name=rfbD {ECO:0000313|EMBL:ABI93427.1};
GN   OrderedLocusNames=RD1_B0018 {ECO:0000313|EMBL:ABI93427.1};
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OG   Plasmid pTB2 {ECO:0000313|EMBL:ABI93427.1,
OG   ECO:0000313|Proteomes:UP000007029}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451 {ECO:0000313|EMBL:ABI93427.1, ECO:0000313|Proteomes:UP000007029};
RN   [1] {ECO:0000313|EMBL:ABI93427.1, ECO:0000313|Proteomes:UP000007029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029};
RC   PLASMID=pTB2 {ECO:0000313|EMBL:ABI93427.1,
RC   ECO:0000313|Proteomes:UP000007029};
RX   PubMed=17098896; DOI=10.1128/JB.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000465; ABI93427.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07GH2; -.
DR   KEGG; rde:RD1_B0018; -.
DR   eggNOG; COG1091; Bacteria.
DR   HOGENOM; CLU_045518_1_0_5; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000007029; Plasmid pTB2.
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:ABI93427.1}; Plasmid {ECO:0000313|EMBL:ABI93427.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007029}.
FT   DOMAIN          27..305
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   307 AA;  32092 MW;  258C15844257D131 CRC64;
     MVSRQRRLVA RPANPRWGGR TVGRAPMKIL VFGQTGQVAT ELAQLDGVTC LGREQADLSD
     PGACEAVIAG CDADAVINAA AYTAVDKAEE DRDTAMIVNA MAPTAMAAAA AARGIPFVHI
     STDYVFDGSG QRPWQPDAPT GPLGVYGASK LGGEKGVAAA GGAHAILRTS WVFSAHGANF
     VKTMRRLGAE RDALTIVADQ IGGPTPARDI AAVCVEIARA LTQDPSKSGT YHFSGAPDIS
     WADFAREIFA QSGLSVDVTD IPTSQYPTPA QRPLNSRLDC STTTATFGIP RPDWRTGLAG
     VLSDLNT
//
DBGET integrated database retrieval system