ID A9Y3F6_CROSK Unreviewed; 300 AA.
AC A9Y3F6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=rmlD {ECO:0000313|EMBL:ABX51886.1};
OS Cronobacter sakazakii (Enterobacter sakazakii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=28141 {ECO:0000313|EMBL:ABX51886.1};
RN [1] {ECO:0000313|EMBL:ABX51886.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCTC 8155 {ECO:0000313|EMBL:ABX51886.1};
RX PubMed=18441119; DOI=10.1128/AEM.02302-07;
RA Mullane N., O'Gaora P., Nally J.E., Iversen C., Whyte P., Wall P.G.,
RA Fanning S.;
RT "Molecular analysis of the Enterobacter sakazakii O-antigen gene locus.";
RL Appl. Environ. Microbiol. 74:3783-3794(2008).
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; EU076546; ABX51886.1; -; Genomic_DNA.
DR AlphaFoldDB; A9Y3F6; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
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 4..294
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 300 AA; 33059 MW; 086695006EBEC137 CRC64;
MKVNILLFGK NGQVGWELQR ALAPLGNLIS LDFNSEDYCG DFSNPEGVAE TVRRIKPDVI
VNAAAHTAVD KAESEREFAQ LLNATSVEAI AREAAKINAW LIHYSTDYVF PGTGETPWCE
SDATAPLNVY GETKLAGEQA VQRFCPNHLI FRTSWVYAGK GNNFAKTMLR LAKERESLSV
INDQYGAPTG AELLADCTAH AIRVALTKPD VAGLYHLVAS GVTTWYDFAA LVFDQARKAG
ITLKLTDLQP VPTSAYPTPA CRPQNSRLNT MKFQQQFGLV LPQWDMGVKR MLEEWFTAGI
//
