ID A0A370G120_GLULI Unreviewed; 302 AA.
AC A0A370G120;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=rfbD {ECO:0000313|EMBL:MBB2187528.1};
GN ORFNames=C7453_106158 {ECO:0000313|EMBL:RDI37435.1}, HLH32_14310
GN {ECO:0000313|EMBL:MBB2187528.1};
OS Gluconacetobacter liquefaciens (Acetobacter liquefaciens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=89584 {ECO:0000313|EMBL:RDI37435.1, ECO:0000313|Proteomes:UP000254958};
RN [1] {ECO:0000313|EMBL:RDI37435.1, ECO:0000313|Proteomes:UP000254958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5603 {ECO:0000313|EMBL:RDI37435.1,
RC ECO:0000313|Proteomes:UP000254958};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB2187528.1, ECO:0000313|Proteomes:UP000562982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 1382 {ECO:0000313|EMBL:MBB2187528.1,
RC ECO:0000313|Proteomes:UP000562982};
RA Sombolestani A.;
RT "Description of novel Gluconacetobacter.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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:RDI37435.1}.
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DR EMBL; JABEQI010000009; MBB2187528.1; -; Genomic_DNA.
DR EMBL; QQAW01000006; RDI37435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370G120; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000254958; Unassembled WGS sequence.
DR Proteomes; UP000562982; 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 ECO:0000313|EMBL:MBB2187528.1}.
FT DOMAIN 11..296
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 302 AA; 31901 MW; 3234131F67D23AAE CRC64;
MNTAQARLSP ILVVGRSGQL ATALGRTDRS DIHCLGRPDI DFDRPETLAA AFAALSPALV
VNAAAWTAVD AAESDPKGAA RANCDGPALL ARLCAARGIP LIHVSTDYVF DGTKGAPYVE
SDPISPRTVY GRSKAEGERA ILAAHGRAII LRTAWVYSPY GRNFVRTMLN AGMKNPVLRV
VGDQLGNPTS ADDLADAILA IIDTIGRTGW HDDYAGLFHA AGSGETTWHG LAVAALQEAA
KAGQPMPEVL AIGTADWPTP AARPQDSRLD CTRLHDVFGI RLPDWRDGVA RSVARLMAVP
AA
//
