ID B6EHC8_ALISL Unreviewed; 293 AA.
AC B6EHC8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 Name=rmlD {ECO:0000313|EMBL:CAQ80704.1};
GN OrderedLocusNames=VSAL_I3020 {ECO:0000313|EMBL:CAQ80704.1};
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ80704.1, ECO:0000313|Proteomes:UP000001730};
RN [1] {ECO:0000313|EMBL:CAQ80704.1, ECO:0000313|Proteomes:UP000001730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ80704.1,
RC ECO:0000313|Proteomes:UP000001730};
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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; FM178379; CAQ80704.1; -; Genomic_DNA.
DR RefSeq; WP_012551416.1; NC_011312.1.
DR AlphaFoldDB; B6EHC8; -.
DR KEGG; vsa:VSAL_I3020; -.
DR eggNOG; COG1091; Bacteria.
DR HOGENOM; CLU_045518_1_0_6; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000001730; Chromosome 1.
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,
KW ECO:0000313|EMBL:CAQ80704.1}.
FT DOMAIN 1..288
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 293 AA; 31782 MW; A74D9557936DF9E5 CRC64;
MRVLITGCYG QVGHCLTAQL VNKASTSVLA LDRDQLDITN QDAVNAIADD FQPTIIINAA
AHTAVDKAED EVDLSYAINR DGPNYLAQAA QRVGAAMLHI STDYVFEGNK VGEYDERDVT
HPQGVYGESK LAGESAVANA CDKHIILRTA WVFGEHGNNF VKTMLRLGVT RDELSIVGDQ
FGGPTYAGDI ANALITIAER ITQGNMVDYG VYHYSGLPHV SWYEFADAIF DTAKEQGVIK
TKPSLTGITT VQYPTPAKRP SNSCLNTNKI TTAFSIEASD WQTALKNIQA YTG
//
