ID   E1V5N8_HALED            Unreviewed;       297 AA.
AC   E1V5N8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 2.
DT   27-MAR-2024, entry version 55.
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=HELO_1267 {ECO:0000313|EMBL:CBV41150.2};
OS   Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS   / 1H9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV41150.2, ECO:0000313|Proteomes:UP000008707};
RN   [1] {ECO:0000313|Proteomes:UP000008707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC   {ECO:0000313|Proteomes:UP000008707};
RX   PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA   Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA   Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA   Kunte H.J.;
RT   "A blueprint of ectoine metabolism from the genome of the industrial
RT   producer Halomonas elongata DSM 2581(T).";
RL   Environ. Microbiol. 13:1973-1994(2011).
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; FN869568; CBV41150.2; -; Genomic_DNA.
DR   AlphaFoldDB; E1V5N8; -.
DR   STRING; 768066.HELO_1267; -.
DR   KEGG; hel:HELO_1267; -.
DR   eggNOG; COG1091; Bacteria.
DR   OrthoDB; 9803892at2; -.
DR   Proteomes; UP000008707; Chromosome.
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}.
FT   DOMAIN          64..278
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   297 AA;  32657 MW;  4B65527C315103A8 CRC64;
     MKLLILDAGH CLSLALARES NRRSDVELVI EPGLDLAPER LDEVAPDALI IPPLSHPISA
     DPSAVTAHAE AVEACMRACR ERDVPLVWCV SDQLYEEGFE GVIDEHVVPQ PRDEGLRRLV
     STGERIRAEL PRHLIVRVGP LFALEGSHAW LGELLDSLAN GEEVRAASDV IFCPTSSDAV
     AMALIGMLQQ QHCGADAWGS YHLAGTEPVS AYTFVSMVRT QLATRLEGRG ESVELGSVKA
     LSHHHDQPLR RVLNCRRVLE VFGVHQKPWR LEVGRMLDLW CLARDEDAGT EEEPGKA
//