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Database: UniProt
Entry: C2EPQ0_9LACO
LinkDB: C2EPQ0_9LACO
Original site: C2EPQ0_9LACO 
ID   C2EPQ0_9LACO            Unreviewed;       326 AA.
AC   C2EPQ0;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   Name=rfbD {ECO:0000313|EMBL:EEJ71489.1};
GN   ORFNames=HMPREF0548_1646 {ECO:0000313|EMBL:EEJ71489.1};
OS   Lactobacillus ultunensis DSM 16047.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=525365 {ECO:0000313|EMBL:EEJ71489.1, ECO:0000313|Proteomes:UP000005583};
RN   [1] {ECO:0000313|EMBL:EEJ71489.1, ECO:0000313|Proteomes:UP000005583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16047 {ECO:0000313|EMBL:EEJ71489.1,
RC   ECO:0000313|Proteomes:UP000005583};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-2009) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEJ71489.1}.
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DR   EMBL; ACGU01000072; EEJ71489.1; -; Genomic_DNA.
DR   RefSeq; WP_007126141.1; NZ_GG693254.1.
DR   AlphaFoldDB; C2EPQ0; -.
DR   STRING; 525365.HMPREF0548_1646; -.
DR   PATRIC; fig|525365.8.peg.1392; -.
DR   eggNOG; COG1091; Bacteria.
DR   HOGENOM; CLU_045518_1_2_9; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000005583; Unassembled WGS sequence.
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   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   ECO:0000313|EMBL:EEJ71489.1}.
FT   DOMAIN          1..317
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   326 AA;  36140 MW;  D2E5E20B71CDAD49 CRC64;
     MKVFVTGVNG QLGHDVMNEL AKRGYEGVGS DLKPEYAGVA DGSAVTKMPY VPLDITDGAA
     VEKVITDVDP DVIVHCAAWT AVDMAEDDDK VAAVRKVNVG GTQNIANVAK KLDVPMVYLS
     TDYVFDGQGT EPWKPDFKGY KPLNVYGETK LGGEKAVSDT LDKYFIVRIA WVFGVNGHNF
     IKTMLKVGAT HDEVKVVNDQ IGTPTYTFDL ARLLVDMIET DKYGYYHVTN SELPATKSGF
     DENGTKTGYI SWYDFTKEIY RQAGYTTKVT PVTTAEYGLS KAVRPFNSRL DKSKLVENGF
     KPLSTWPHAV HRYLEILKKQ GFFDEL
//
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