ID Q8Y834_LISMO Unreviewed; 276 AA.
AC Q8Y834;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN OrderedLocusNames=lmo1084 {ECO:0000313|EMBL:CAC99162.1};
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963 {ECO:0000313|EMBL:CAC99162.1, ECO:0000313|Proteomes:UP000000817};
RN [1] {ECO:0000313|EMBL:CAC99162.1, ECO:0000313|Proteomes:UP000000817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817};
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D.,
RA Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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}.
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DR EMBL; AL591977; CAC99162.1; -; Genomic_DNA.
DR PIR; AD1210; AD1210.
DR RefSeq; NP_464609.1; NC_003210.1.
DR RefSeq; WP_003721501.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y834; -.
DR STRING; 169963.gene:17593740; -.
DR PaxDb; 169963-lmo1084; -.
DR EnsemblBacteria; CAC99162; CAC99162; CAC99162.
DR GeneID; 986256; -.
DR KEGG; lmo:lmo1084; -.
DR PATRIC; fig|169963.11.peg.1114; -.
DR eggNOG; COG1091; Bacteria.
DR HOGENOM; CLU_045518_1_2_9; -.
DR OrthoDB; 9803892at2; -.
DR PhylomeDB; Q8Y834; -.
DR BioCyc; LMON169963:LMO1084-MONOMER; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IBA:GO_Central.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IBA:GO_Central.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IBA:GO_Central.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000817}.
FT DOMAIN 1..274
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 276 AA; 31170 MW; 55B15236ECBD3A99 CRC64;
MSILVTGANG QLGTELVQLL KEHNLTVTEW DKDSVDIVDK AAVKKAMLDL KPEWIIHCAA
FTNVEAAEDE LKNVNWEVNV DGTENISEAA EIVGAKLVYI STDYVFDGTK KEAYLPDDKT
NPLNQYGIAK LAGEKVALEK NSQTYVIRTS WVFGKYGNNF VYSMLKLAET HKELKVVNDQ
LGRPTYTYDL ADFIRFVIEK NPAYGIYQFS NSGTATWFEF ATEILKDKDV TVNPCTSDEF
PQKAERPKTS IMSLEKVEKL GFNIPTWQDA LVRFKK
//
