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Database: UniProt
Entry: Q8DYQ0_STRA5
LinkDB: Q8DYQ0_STRA5
Original site: Q8DYQ0_STRA5 
ID   Q8DYQ0_STRA5            Unreviewed;       284 AA.
AC   Q8DYQ0;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 87.
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:AAN00294.1};
GN   OrderedLocusNames=SAG1424 {ECO:0000313|EMBL:AAN00294.1};
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435 {ECO:0000313|EMBL:AAN00294.1, ECO:0000313|Proteomes:UP000000821};
RN   [1] {ECO:0000313|EMBL:AAN00294.1, ECO:0000313|Proteomes:UP000000821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R {ECO:0000313|Proteomes:UP000000821};
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin S., Kolonay J.F., Umayam L.A., Madupu R., Lewis M.R.,
RA   Radune D., Fedorova N.B., Scanlan D., Khouri H., Mulligan S., Carty H.A.,
RA   Cline R.T., Gill J., Scarselli M., Mora M., Iacobini E.T., Brettoni C.,
RA   Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., Rappuoli R.,
RA   Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; AE009948; AAN00294.1; -; Genomic_DNA.
DR   RefSeq; NP_688421.1; NC_004116.1.
DR   RefSeq; WP_000600896.1; NC_004116.1.
DR   AlphaFoldDB; Q8DYQ0; -.
DR   STRING; 208435.SAG1424; -.
DR   GeneID; 66886302; -.
DR   KEGG; sag:SAG1424; -.
DR   PATRIC; fig|208435.3.peg.1432; -.
DR   HOGENOM; CLU_045518_1_2_9; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000000821; 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   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:UP000000821}.
FT   DOMAIN          2..280
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   284 AA;  32310 MW;  2934B0A73B5EE098 CRC64;
     MILITGANGQ LGSELRHLLD ERTQEYVAVD VAEMDITNAE MVDKVFEEVK PSLVYHCAAY
     TAVDAAEDEG KELDFAINVT GTENVAKAAA KHDATLVYIS TDYVFDGEKP VGQEWEVDDL
     PDPKTEYGRT KRMGEELVEK YTSKFYTIRT AWVFGNYGKN FVFTMQNLAK THKTLTVVND
     QHGRPTWTRT LAEFMTYLAE NQKDFGYYHL SNDAKEDTTW YDFAVEILKD TDVEVKPVDS
     SQFPAKAKRP LNSTMSLEKA KATGFVIPTW QDALKEFYKQ EVKK
//
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