ID A0A1G1Y0Y7_9BACT Unreviewed; 283 AA.
AC A0A1G1Y0Y7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=A2744_02165 {ECO:0000313|EMBL:OGY45470.1};
OS Candidatus Buchananbacteria bacterium RIFCSPHIGHO2_01_FULL_44_11.
OC Bacteria; Candidatus Buchananbacteria.
OX NCBI_TaxID=1797535 {ECO:0000313|EMBL:OGY45470.1, ECO:0000313|Proteomes:UP000178240};
RN [1] {ECO:0000313|EMBL:OGY45470.1, ECO:0000313|Proteomes:UP000178240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGY45470.1}.
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DR EMBL; MHIE01000019; OGY45470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1Y0Y7; -.
DR STRING; 1797535.A2744_02165; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000178240; 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 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..283
FT /note="dTDP-4-dehydrorhamnose reductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009581465"
FT DOMAIN 7..279
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 283 AA; 31702 MW; B8C6B8AB7A6D3679 CRC64;
MVCMTKKVLI LGAKGMLGQA LARVFSDADL SLWDLNQLDI TDQQQVEQKI LSLQPQIIIN
AAAYTDVDGC ETNEDLAVRV NGLAVGYLAS VAKHLGAILV HYSTDYVFDG QNSAGYKESD
PTNPVNAYGR TKLRGEQELT KKGEKYYLIR TAWLYGPGGK NFVDTILTKA KSSDKLKVVN
DQFGKPTYTL DLAQATRNIV EQNQPFGIYH ITNQAPASGI TWYEFAQAAV KLKNLSAEIE
PCSTEEFPRP AQRPKYSMLI NTKIKPMREW QEALNDYLKY NYE
//