GenomeNet

Database: UniProt
Entry: E6J8T5_9ACTN
LinkDB: E6J8T5_9ACTN
Original site: E6J8T5_9ACTN 
ID   E6J8T5_9ACTN            Unreviewed;       109 AA.
AC   E6J8T5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
DE   Flags: Fragment;
GN   ORFNames=ES5_08171 {ECO:0000313|EMBL:EFV91997.1};
OS   Dietzia cinnamea P4.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC   Dietzia.
OX   NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV91997.1, ECO:0000313|Proteomes:UP000004165};
RN   [1] {ECO:0000313|EMBL:EFV91997.1, ECO:0000313|Proteomes:UP000004165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P4 {ECO:0000313|EMBL:EFV91997.1,
RC   ECO:0000313|Proteomes:UP000004165};
RX   PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA   Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA   Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT   "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT   survival in complex tropical soil habitats and biotechnology potential.";
RL   Antonie Van Leeuwenhoek 101:289-302(2012).
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:EFV91997.1}.
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; AEKG01000159; EFV91997.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6J8T5; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000004165; 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          17..109
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
FT   NON_TER         109
FT                   /evidence="ECO:0000313|EMBL:EFV91997.1"
SQ   SEQUENCE   109 AA;  11486 MW;  59FB8A0B05E96130 CRC64;
     MNADDEGAAA RPDALPRVLV TGGRGQLGTH LRLAHPGEVL APGRDELDIT RAESVAGYLD
     RHQPAVVINA AAYTDVDGAE TDESGAHLVN VEGPRILAEA CRERGLRLV
//
DBGET integrated database retrieval system