CURA_ECOLI
ID CURA_ECOLI Reviewed; 345 AA.
AC P76113; P78255;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=NADPH-dependent curcumin reductase;
DE EC=1.3.1.n3;
DE AltName: Full=NADPH-dependent curcumin/dihydrocurcumin reductase;
GN Name=curA; Synonyms=yncB; OrderedLocusNames=b1449, JW5907;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION AS A CURCUMIN REDUCTASE, CATALYTIC ACTIVITY, MASS SPECTROMETRY,
RP MUTAGENESIS OF CYS-247, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND NOMENCLATURE.
RX PubMed=21467222; DOI=10.1073/pnas.1016217108;
RA Hassaninasab A., Hashimoto Y., Tomita-Yokotani K., Kobayashi M.;
RT "Discovery of the curcumin metabolic pathway involving a unique enzyme in
RT an intestinal microorganism.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:6615-6620(2011).
CC -!- FUNCTION: Catalyzes the metal-independent reduction of curcumin to
CC dihydrocurcumin (DHC) as an intermediate product, followed by further
CC reduction to tetrahydrocurcumin (THC) as an end product. It also acts
CC on 3-octene-2-one, 3-hepten-2-one, resveratrol, and trans-2-octenal.
CC {ECO:0000269|PubMed:21467222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 NADP(+) + tetrahydrocurcumin = curcumin + 2 H(+) + 2 NADPH;
CC Xref=Rhea:RHEA:34815, ChEBI:CHEBI:3962, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67263; EC=1.3.1.n3;
CC Evidence={ECO:0000269|PubMed:21467222};
CC -!- ACTIVITY REGULATION: Inhibited by thiol-specific reagents (p-
CC chloromercuribenzoate and 5,5'-dithio-bis-2-nitrobenzoate).
CC {ECO:0000269|PubMed:21467222}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29 uM for curcumin {ECO:0000269|PubMed:21467222};
CC Vmax=9.35 umol/min/mg enzyme {ECO:0000269|PubMed:21467222};
CC pH dependence:
CC Optimum pH is 5.9. The enzyme is most stable in the pH range of 4.5
CC to 12.0, with 90% of the initial activity being retained even at pH
CC 12.0. {ECO:0000269|PubMed:21467222};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius. The enzyme is most stable
CC from 10 to 50 degrees Celsius. {ECO:0000269|PubMed:21467222};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21467222}.
CC -!- MASS SPECTROMETRY: Mass=37513; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21467222};
CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74531.4; -; Genomic_DNA.
DR EMBL; AP009048; BAA15081.1; -; Genomic_DNA.
DR PIR; D64897; D64897.
DR RefSeq; NP_415966.6; NC_000913.3.
DR RefSeq; WP_000531462.1; NZ_SSZK01000021.1.
DR AlphaFoldDB; P76113; -.
DR SMR; P76113; -.
DR BioGRID; 4260195; 14.
DR DIP; DIP-12748N; -.
DR STRING; 511145.b1449; -.
DR jPOST; P76113; -.
DR PaxDb; P76113; -.
DR PRIDE; P76113; -.
DR EnsemblBacteria; AAC74531; AAC74531; b1449.
DR EnsemblBacteria; BAA15081; BAA15081; BAA15081.
DR GeneID; 946012; -.
DR KEGG; ecj:JW5907; -.
DR KEGG; eco:b1449; -.
DR PATRIC; fig|1411691.4.peg.819; -.
DR EchoBASE; EB3534; -.
DR eggNOG; COG2130; Bacteria.
DR InParanoid; P76113; -.
DR PhylomeDB; P76113; -.
DR BioCyc; EcoCyc:G6760-MON; -.
DR BioCyc; MetaCyc:G6760-MON; -.
DR PRO; PR:P76113; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR041694; ADH_N_2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR045010; MDR_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43205; PTHR43205; 1.
DR Pfam; PF16884; ADH_N_2; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..345
FT /note="NADPH-dependent curcumin reductase"
FT /id="PRO_0000218075"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 160..163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 182..186
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 247..253
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 282..284
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MUTAGEN 247
FT /note="C->A: Exhibits a reduction of about 50% in activity,
FT but is not inhibited by 5,5'-dithio-bis-2-nitrobenzoate."
FT /evidence="ECO:0000269|PubMed:21467222"
SQ SEQUENCE 345 AA; 37610 MW; CED3CF29B60E246F CRC64;
MGQQKQRNRR WVLASRPHGA PVPENFRLEE DDVATPGEGQ VLLRTVYLSL DPYMRGRMSD
EPSYSPPVDI GGVMVGGTVS RVVESNHPDY QSGDWVLGYS GWQDYDISSG DDLVKLGDHP
QNPSWSLGVL GMPGFTAYMG LLDIGQPKEG ETLVVAAATG PVGATVGQIG KLKGCRVVGV
AGGAEKCRHA TEVLGFDVCL DHHADDFAEQ LAKACPKGID IYYENVGGKV FDAVLPLLNT
SARIPVCGLV SSYNATELPP GPDRLPLLMA TVLKKRIRLQ GFIIAQDYGH RIHEFQREMG
QWVKEDKIHY REEITDGLEN APQTFIGLLK GKNFGKVVIR VAGDD
