ID L9U765_9GAMM Unreviewed; 297 AA.
AC L9U765;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ORFNames=HALTITAN_2810 {ECO:0000313|EMBL:ELY20456.1};
OS Halomonas titanicae BH1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1204738 {ECO:0000313|EMBL:ELY20456.1, ECO:0000313|Proteomes:UP000011651};
RN [1] {ECO:0000313|EMBL:ELY20456.1, ECO:0000313|Proteomes:UP000011651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH1 {ECO:0000313|EMBL:ELY20456.1,
RC ECO:0000313|Proteomes:UP000011651};
RX PubMed=23516210;
RA Sanchez-Porro C., de la Haba R.R., Cruz-Hernandez N., Gonzalez J.M.,
RA Reyes-Guirao C., Navarro-Sampedro L., Carballo M., Ventosa A.;
RT "Draft Genome of the Marine Gammaproteobacterium Halomonas titanicae.";
RL Genome Announc. 1:E0008313-E0008313(2013).
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}.
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:ELY20456.1}.
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DR EMBL; AOPO01000017; ELY20456.1; -; Genomic_DNA.
DR RefSeq; WP_009288278.1; NZ_AOPO01000017.1.
DR AlphaFoldDB; L9U765; -.
DR PATRIC; fig|1204738.3.peg.4242; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000011651; 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 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..293
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 297 AA; 32328 MW; E309203774C78A39 CRC64;
MNIFITGGNG QVGFELQRQF SLFGNVLAPT RHELDLTDAN AVDAYLAEHQ PALILNAGAY
TAVDKAESEP AQAKRLNAEL PAQLAEYAAK HNIPLVHYST DYVYPGDGET PWQEDSPTAP
LSVYGQTKLE GDQSVTQSGC QHLIFRTSWV YAARGNNFMK TMLRLGRERD ALSIVNDQIG
APTPARLIAQ VTALAFTPHN SPLTPHITSG IYHLAPRGET SWHGFASEIF KQAQVLGEEL
ATQSGTVSGI PTVEFPTPAQ RPLNSRMRLT KLEAALGVTL PVWQHQLALT LAECCEA
//
