ID R4K7W3_CLOPA Unreviewed; 279 AA.
AC R4K7W3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=Clopa_1669 {ECO:0000313|EMBL:AGK96594.1};
OS Clostridium pasteurianum BC1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK96594.1, ECO:0000313|Proteomes:UP000013523};
RN [1] {ECO:0000313|EMBL:AGK96594.1, ECO:0000313|Proteomes:UP000013523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC1 {ECO:0000313|EMBL:AGK96594.1,
RC ECO:0000313|Proteomes:UP000013523};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J.,
RA Taghavi S., Francis A., van der Lelie D., Woyke T.;
RT "Complete sequence of chromosome of Clostridium pasteurianum BC1.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003261; AGK96594.1; -; Genomic_DNA.
DR RefSeq; WP_015614913.1; NC_021182.1.
DR AlphaFoldDB; R4K7W3; -.
DR STRING; 86416.Clopa_1669; -.
DR KEGG; cpas:Clopa_1669; -.
DR PATRIC; fig|86416.3.peg.1645; -.
DR eggNOG; COG1091; Bacteria.
DR HOGENOM; CLU_045518_1_2_9; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000013523; 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 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 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:UP000013523}.
FT DOMAIN 1..274
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 279 AA; 32007 MW; C44F839A3A5A44C5 CRC64;
MKILITGAEN PLSNYIENRF KGTNEIYSFT RNELDISDKN LTYEIITDNK PDILIHLDSM
SNIDICEHDE SLAYTINTIG TLNVAYPCSI LNIPIIFLST SYVYDGNKNS PYFETDKCSP
VNIYGKTKLA GEKLIRTLCK KYFIVRTGWI FGEENCFVNK VLNNSNVSMF VCSTETGNPT
YVEDLCRVIE KMFNSNLYGI YNCGNPSSTT KSAWVKKIFN YAGIERRILE MPENFLRNTA
IRPKNSSLNI SLIKNCFDIE LPNWESRLSE YINDKLKNQ
//
