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
//