ID A0A0L0LJN7_9BACT Unreviewed; 281 AA.
AC A0A0L0LJN7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=AB198_02620 {ECO:0000313|EMBL:KND50211.1};
OS Parcubacteria bacterium C7867-003.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659197 {ECO:0000313|EMBL:KND50211.1, ECO:0000313|Proteomes:UP000036964};
RN [1] {ECO:0000313|EMBL:KND50211.1, ECO:0000313|Proteomes:UP000036964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-003 {ECO:0000313|EMBL:KND50211.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(2015).
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}.
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:KND50211.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFCM01000015; KND50211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LJN7; -.
DR STRING; 1659197.AB198_02620; -.
DR Proteomes; UP000036964; Unassembled WGS sequence.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:RHEA.
DR GO; GO:0050377; F:UDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:KND50211.1}; NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082}.
FT DOMAIN 1..271
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 281 AA; 31580 MW; 30B5810EC8B1F3A8 CRC64;
MKIYILGASG FMGSGMAEYL KSKGNEVFTE RVDVTDLSKL REVFNKTKPE VVINFAGVRA
YPNIDWCEDH KQETVAVNVS GAINAMLSAI EVGAYPIQIS SGCVYSGDVS QEFTEDDIPN
FHGSFYSRMR IVLENSLKEL PVLYLRLRMP ISYKSNPRNT INKIISYTRV ISVPNSVTLV
EDMYPAIEHL INKKVLGVLN LTNEGYVTHG QILEAYKKHV KPDHNFELIT PEELEKSVTK
TGRSNCVLSM EKAKSLGVVM PAVDEKRLEE IMLQLKQTLN I
//
