ID A0A1L7CRE3_9CORY Unreviewed; 350 AA.
AC A0A1L7CRE3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=CFRA_02940 {ECO:0000313|EMBL:APT88402.1};
OS Corynebacterium frankenforstense DSM 45800.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1437875 {ECO:0000313|EMBL:APT88402.1, ECO:0000313|Proteomes:UP000185434};
RN [1] {ECO:0000313|EMBL:APT88402.1, ECO:0000313|Proteomes:UP000185434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST18 {ECO:0000313|EMBL:APT88402.1,
RC ECO:0000313|Proteomes:UP000185434};
RA Ruckert C., Albersmeier A., Winkler A., Lipski A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium frankenforstense ST18(T) (=DSM
RT 45800(T)), isolated from raw cow milk.";
RL Submitted (AUG-2014) 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|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}.
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DR EMBL; CP009247; APT88402.1; -; Genomic_DNA.
DR RefSeq; WP_075663381.1; NZ_CP009247.1.
DR AlphaFoldDB; A0A1L7CRE3; -.
DR STRING; 1437875.CFRA_02940; -.
DR KEGG; cfk:CFRA_02940; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000185434; Chromosome.
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; 2.
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 PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR Pfam; PF04321; RmlD_sub_bind; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW Reference proteome {ECO:0000313|Proteomes:UP000185434}.
FT DOMAIN 1..111
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT DOMAIN 160..346
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT REGION 132..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 35471 MW; 6E7AA77662C3FB16 CRC64;
MRVVVTGARG QLGRSLALTC PPGLDGDVVW ADRSLLDVTD PAAVAASPAL AGADVVLNCA
AFTDVDGAEE EPGRTSAEAA NATAPGLIAR RCAEEGARLV HVSTDYVFGD AVLDDAAHAD
AAGSRPVLDD AAPGGVAGSE GVAGSEGVAG SGAAVPAGAR PLLPGDPTSP QTVYGRTKLA
GERAALAACP QTTVVRTAWV YSGDTLPEHK DFVSTMLRLA RGGVDPKVVD DQFGSPTFAP
DLARALWRLV LEGGGAAAAA AADAVGAAHA GTDTDTAGRV LHGVGAGWTS WYLLAREVFA
AAGFDPDRVS PVDTAGYPTR AKRPRWSVLA PDLELPEWRT GVARAVAARL
//