ID A0A1F6P9M9_9BACT Unreviewed; 280 AA.
AC A0A1F6P9M9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=A2563_04450 {ECO:0000313|EMBL:OGH92887.1};
OS Candidatus Magasanikbacteria bacterium RIFOXYD1_FULL_40_23.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798705 {ECO:0000313|EMBL:OGH92887.1, ECO:0000313|Proteomes:UP000176634};
RN [1] {ECO:0000313|EMBL:OGH92887.1, ECO:0000313|Proteomes:UP000176634}
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:OGH92887.1}.
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DR EMBL; MFRA01000005; OGH92887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6P9M9; -.
DR STRING; 1798705.A2563_04450; -.
DR Proteomes; UP000176634; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 31..275
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 280 AA; 31061 MW; 1BE2DE43D9C863B3 CRC64;
MKTKKILIIG NGFLGRKCAT AWPDAILSDK KISSVKDVED LLDEHKPDSV LNAAGVVGKP
NVDWCETHQM ETILGNTVLP IMIAEACQNK GVYLLHMGTG CVFYGYSSDS EGWKEEDVAN
PSAVYTRTKY AADLVLSTLP NIGIARIRMP IDSQSTPANL IDKLSSYARV VDVVNSVTVV
DDMVDVFKQL LEKQASGIFH VTNPGAIKHK EILEMYKEFV DPDHKNEWIT ERELVTSGLA
KKTRSNNILQ SNNLEKLGIK MRPVKEAVLD VLKKYASLKK
//