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Database: UniProt
Entry: E2MUB7_CORAY
LinkDB: E2MUB7_CORAY
Original site: E2MUB7_CORAY 
ID   E2MUB7_CORAY            Unreviewed;       324 AA.
AC   E2MUB7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   Name=rfbD {ECO:0000313|EMBL:EEB63755.1};
GN   ORFNames=CORAM0001_0348 {ECO:0000313|EMBL:EEB63755.1};
OS   Corynebacterium amycolatum SK46.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=553204 {ECO:0000313|EMBL:EEB63755.1, ECO:0000313|Proteomes:UP000003275};
RN   [1] {ECO:0000313|EMBL:EEB63755.1, ECO:0000313|Proteomes:UP000003275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK46 {ECO:0000313|EMBL:EEB63755.1,
RC   ECO:0000313|Proteomes:UP000003275};
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (NOV-2008) 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}.
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:EEB63755.1}.
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DR   EMBL; ABZU01000002; EEB63755.1; -; Genomic_DNA.
DR   RefSeq; WP_005509826.1; NZ_ABZU01000002.1.
DR   AlphaFoldDB; E2MUB7; -.
DR   eggNOG; COG1091; Bacteria.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000003275; 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:EEB63755.1}.
FT   DOMAIN          24..323
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   324 AA;  34781 MW;  A89C796F9BFD1EB4 CRC64;
     MSEISVSHFA THGPTCSNSR RPIIAITGAA GQLGTALQRD SFAADVEVRA LTRAQLDITD
     SAAVEATPLL DDVDIIISAA AATDVDGAES DPGSAHLINA LGPKYLAARA KKEDAYLIHI
     STDYVFGDVA IDEMTGQRRA LRVDDFTAPQ TMYGRTKLVG ENNVRDSGAR FAILRTAWVW
     SGPTQPEAKD FVSTMMRLAE TATDDKGNPA IIKVVDDQHG NPTFVGALAG AIWELSERVL
     SEPNSAPTGT FHVTGSGQAT WFEVAREVFR LTGHDPQRVV ACTSSEFPRP APRPAWSVLD
     GSAWSEVGLH SLPEWQDTLR AVLT
//
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