ID A0A0G1C5I1_9BACT Unreviewed; 291 AA.
AC A0A0G1C5I1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=UV07_C0001G0023 {ECO:0000313|EMBL:KKS44903.1};
OS Candidatus Azambacteria bacterium GW2011_GWB1_42_17.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1618615 {ECO:0000313|EMBL:KKS44903.1, ECO:0000313|Proteomes:UP000033986};
RN [1] {ECO:0000313|EMBL:KKS44903.1, ECO:0000313|Proteomes:UP000033986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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:KKS44903.1}.
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DR EMBL; LCDB01000001; KKS44903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1C5I1; -.
DR PATRIC; fig|1618615.3.peg.23; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000033986; 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}.
FT DOMAIN 6..285
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 291 AA; 32337 MW; C28AC4F6D65A0379 CRC64;
MKYKLVLIIG STGLLAFDLI RIFKEDDSYK VIGSNHDDFD VADKQATEKF IALINPDIVI
NTAGFIKVDE CERDPKKSFK VNAIGAHNVA AAAKAISAVN IYISTSYIFD GNKKSFSENS
VPNPVNIYGA SKLAGEILTK IIGGKYYIIR TSWLYGIRRQ DSDFIAQVIE PAKKGEAIKV
IIDQFGTLTY TLDLALKIKE LIDKKASSGV YHITNSGSSS WRGFAEKIIK SCKIHAKLIS
VKLAERSPII KKPKYSVLTS VNLKKAGIQK LRPWEEALKD YLTEIRDSLI L
//
