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Database: UniProt
Entry: I5CKR4_9BURK
LinkDB: I5CKR4_9BURK
Original site: I5CKR4_9BURK 
ID   I5CKR4_9BURK            Unreviewed;       303 AA.
AC   I5CKR4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
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   ORFNames=WQE_34041 {ECO:0000313|EMBL:EIM96482.1};
OS   Paraburkholderia hospita BS001.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1171375 {ECO:0000313|EMBL:EIM96482.1};
RN   [1] {ECO:0000313|EMBL:EIM96482.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS001 {ECO:0000313|EMBL:EIM96482.1};
RX   PubMed=22843604; DOI=10.1128/JB.00725-12;
RA   Nazir R., Hansen M.A., Sorensen S., van Elsas J.D.;
RT   "Draft Genome Sequence of the Soil Bacterium Burkholderia terrae Strain
RT   BS001, Which Interacts with Fungal Surface Structures.";
RL   J. Bacteriol. 194:4480-4481(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|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   -!- 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:EIM96482.1}.
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DR   EMBL; AKAU01000193; EIM96482.1; -; Genomic_DNA.
DR   AlphaFoldDB; I5CKR4; -.
DR   PATRIC; fig|1171375.3.peg.7059; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000004980; 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          11..302
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   303 AA;  32645 MW;  D6119ED2DF40EE42 CRC64;
     MRTMTNTTQS TILLTGANGQ VGFELMRSLQ GLGTLVALDR SRLDLADLDQ VRAVTRQIKP
     TLIVNAAAYT AVDRAESEPE LAMLVNGKAP GVLAEEAKRL GAAIIHYSTD YVFDGAKSGP
     YVEDDMVNPQ NAYGRSKLAG ERAVAEAGGA HLVLRTSWVY GRRGSNFLLT MLRLAAERPE
     LRIVADQYGA PTWCASIASL TAHVVAQARA VAARDAADWW SEKSGIYHLT ASGSTSWFGF
     AEAIFELAGQ ERTPKVVPIA TSDYPLPAKR PANSRLLNDK LACAFGLNAP DWRDALRQAL
     AQG
//
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