ID I3UR36_PSEPU Unreviewed; 300 AA.
AC I3UR36;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-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=YSA_02200 {ECO:0000313|EMBL:AFK67957.1};
OS Pseudomonas putida ND6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=231023 {ECO:0000313|EMBL:AFK67957.1, ECO:0000313|Proteomes:UP000005268};
RN [1] {ECO:0000313|EMBL:AFK67957.1, ECO:0000313|Proteomes:UP000005268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND6 {ECO:0000313|EMBL:AFK67957.1,
RC ECO:0000313|Proteomes:UP000005268};
RX PubMed=22933774; DOI=10.1128/JB.01190-12;
RA Li S., Zhao H., Li Y., Niu S., Cai B.;
RT "Complete Genome Sequence of the Naphthalene-Degrading Pseudomonas putida
RT Strain ND6.";
RL J. Bacteriol. 194:5154-5155(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}.
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DR EMBL; CP003588; AFK67957.1; -; Genomic_DNA.
DR RefSeq; WP_014754172.1; NC_017986.1.
DR AlphaFoldDB; I3UR36; -.
DR KEGG; ppi:YSA_02200; -.
DR PATRIC; fig|231023.4.peg.1051; -.
DR HOGENOM; CLU_045518_1_0_6; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000005268; 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 GO; GO:0009243; P:O antigen 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 1..299
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 300 AA; 32276 MW; D8F3AA7A02C873EE CRC64;
MKIVLLGKNG QVGWELQRAL APLGEVIALD RQGAEGLCGD LSNLEALAAT VRQLAPDVIV
NAAAYTAVDK AESDQALAAM INAEAPAVLA REAAALGAWL IHYSTDYVFD GSGNHRWQET
APTGPLSVYG RTKLEGERGI DASGAKAVVL RTSWVYAARG HNFAKTMLRL ATEREALSVV
ADQFGAPTGA ELIADVTAHI LRQIFNGQDN RQLAGIYHLA ASGETSWHGF AQFVLAHAQR
NGVALKVAAD QVVAISTEAY PVPAPRPRNS RLALDKLENT FNFKMPLWEQ GVQRMLDEIQ
//