ID   A0KUZ6_SHESA            Unreviewed;       291 AA.
AC   A0KUZ6;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|ARBA:ARBA00017099, ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|ARBA:ARBA00012929, ECO:0000256|RuleBase:RU364082};
GN   OrderedLocusNames=Shewana3_1381 {ECO:0000313|EMBL:ABK47615.1};
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK47615.1, ECO:0000313|Proteomes:UP000002589};
RN   [1] {ECO:0000313|Proteomes:UP000002589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) 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|ARBA:ARBA00000079,
CC         ECO:0000256|RuleBase:RU364082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364082};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|RuleBase:RU364082};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004781, 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; CP000469; ABK47615.1; -; Genomic_DNA.
DR   RefSeq; WP_011716449.1; NC_008577.1.
DR   AlphaFoldDB; A0KUZ6; -.
DR   STRING; 94122.Shewana3_1381; -.
DR   KEGG; shn:Shewana3_1381; -.
DR   eggNOG; COG1091; Bacteria.
DR   HOGENOM; CLU_045518_1_0_6; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   UniPathway; UPA00281; -.
DR   Proteomes; UP000002589; 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   GO; GO:0009243; P:O antigen 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}.
FT   DOMAIN          1..287
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   291 AA;  31906 MW;  944B77460C3CADBC CRC64;
     MKILVTGSNG QVGSCLVKLL NQIPEIEFLA VDREQLDITD YEAVNKLVSE FKPDAIINAA
     AHTAVDKAEQ EVELSYAINR DGPQFLAQAA NSVGATILHI STDYVFAGDK VGEYVETDEV
     APQGIYGKSK LAGELAVAAA CPRHIIMRTA WVFCETGNNF IKTMLRLAQS RDELGVVADQ
     FGGPTYAGDI ANTLIEIAQA LYAGNTHYGI YHFSGLPHVS WYQFSCQIFK QAKAQKLVSK
     DMLINGISSE QYPTPVKRPA NSKLSCRKIE QTFGVKPCDW QSALNNLMGY F
//