ID A0A196MK62_9SPHN Unreviewed; 295 AA.
AC A0A196MK62;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=A7Q26_20410 {ECO:0000313|EMBL:OAN55680.1};
OS Sphingobium sp. TCM1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=453246 {ECO:0000313|EMBL:OAN55680.1, ECO:0000313|Proteomes:UP000078322};
RN [1] {ECO:0000313|EMBL:OAN55680.1, ECO:0000313|Proteomes:UP000078322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCM1 {ECO:0000313|EMBL:OAN55680.1,
RC ECO:0000313|Proteomes:UP000078322};
RA Takahashi S.;
RT "Draft Genome Sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp.
RT strain TDK1, Haloalkyl Organophosphorus Flame Retardant-Degrading
RT Bacteria.";
RL Submitted (MAY-2016) 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:OAN55680.1}.
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; LXVX01000014; OAN55680.1; -; Genomic_DNA.
DR RefSeq; WP_066859874.1; NZ_LXVX01000014.1.
DR AlphaFoldDB; A0A196MK62; -.
DR STRING; 453246.A7Q26_20410; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000078322; 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; IPR028098; Glyco_trans_4-like_N.
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; PF13579; Glyco_trans_4_4; 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 Reference proteome {ECO:0000313|Proteomes:UP000078322}.
FT DOMAIN 1..290
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT DOMAIN 7..106
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13579"
SQ SEQUENCE 295 AA; 30409 MW; BA779F760F756919 CRC64;
MKIAVTGTAG QVVTSLIERG AAAGHEVVAI GRPDLDLADP ASVVRVLTKA APDVIVSAAA
YTAVDKAEGE SDLAHAVNGA GAGAVAQAAK ALGVPVIHIS TDYVFDGTLD RPYAESDPTG
PTGVYGASKL AGERAVLEGH DNSVALRVAW VYSPFGGNFV KTMLRLAGDR DEVSVVADQH
GNPTSALAIA DGIFQVATNL VADSSPELRG VFHMTAQGEG SWADFAEAIF AASAARGGPS
ATVRRIGTAD YPTPATRPAN SRLDCGRIAR LHGVALPDWH TSLDEVMDRL QPVTH
//
