ID F2I9X4_FLUTR Unreviewed; 301 AA.
AC F2I9X4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN OrderedLocusNames=Fluta_2146 {ECO:0000313|EMBL:AEA44132.1};
OS Fluviicola taffensis (strain DSM 16823 / NCIMB 13979 / RW262).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Crocinitomicaceae; Fluviicola.
OX NCBI_TaxID=755732 {ECO:0000313|EMBL:AEA44132.1, ECO:0000313|Proteomes:UP000007463};
RN [1] {ECO:0000313|EMBL:AEA44132.1, ECO:0000313|Proteomes:UP000007463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16823 / RW262 / RW262 {ECO:0000313|Proteomes:UP000007463};
RX PubMed=22180807; DOI=10.4056/sigs.2124912;
RA Woyke T., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA Mwirichia R., Sikorski J., Tindall B.J., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the gliding freshwater bacterium Fluviicola
RT taffensis type strain (RW262).";
RL Stand. Genomic Sci. 5:21-29(2011).
RN [2] {ECO:0000313|Proteomes:UP000007463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16823 / RW262 / RW262 {ECO:0000313|Proteomes:UP000007463};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Fluviicola taffensis DSM 16823.";
RL Submitted (FEB-2011) 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; CP002542; AEA44132.1; -; Genomic_DNA.
DR RefSeq; WP_013686902.1; NC_015321.1.
DR AlphaFoldDB; F2I9X4; -.
DR STRING; 755732.Fluta_2146; -.
DR KEGG; fte:Fluta_2146; -.
DR eggNOG; COG1091; Bacteria.
DR HOGENOM; CLU_045518_2_1_10; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000007463; 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 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:UP000007463}.
FT DOMAIN 1..296
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 301 AA; 33558 MW; 9451CA0772282AC5 CRC64;
MKILITGSNG LLGQKIVKRC LKHHISFIAT SKGVNRNPEC PSENYIELDL VNSEEVEALI
KAQKPTAIIH TAALTNVDYC ELHPEECYFV NVRASNVLFE AAKKVKAHFQ LLSTDFVFDG
ENGPYKEDDT VNPLSIYAQS KVDAEELLLN DSDTNWSIAR TIIVYGTGFG LSRSNMILWA
LEALPKGEVM KLVDDQFRAP TWADDLAYGC VEIIKRNERG IFHLSGPVTR SVKAIVEEVG
KALELENIAI ETISSTTLNQ AAKRPPRTGF DLSKAAQKLD YLPLDIQESI PLLLRDIDYY
S
//
