ID   TFDF2_CUPPJ             Reviewed;         359 AA.
AC   P94135; Q46M61;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Maleylacetate reductase 2;
DE            EC=1.3.1.32;
DE   AltName: Full=Chloromaleylacetate reductase;
DE   AltName: Full=Maleylacetate reductase II;
GN   Name=tfdFII; OrderedLocusNames=Reut_D6471;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OG   Plasmid pJP4, and Plasmid pPJ4.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RA   van der Meer J.R.;
RL   Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RX   PubMed=15186344; DOI=10.1111/j.1462-2920.2004.00596.x;
RA   Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T.,
RA   Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B.;
RT   "Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha
RT   JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants
RT   and evolution of specialized chloroaromatic degradation pathways.";
RL   Environ. Microbiol. 6:655-668(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197; PLASMID=pPJ4;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-32, AND CHARACTERIZATION.
RC   PLASMID=pJP4;
RX   PubMed=8226615; DOI=10.1128/jb.175.21.6745-6754.1993;
RA   Seibert V., Stadler-Fritzsche K., Schlomann M.;
RT   "Purification and characterization of maleylacetate reductase from
RT   Alcaligenes eutrophus JMP134(pJP4).";
RL   J. Bacteriol. 175:6745-6754(1993).
CC   -!- FUNCTION: Plays a major role in the degradation of chloroaromatic
CC       compounds by channeling maleylacetate and some of its substituted
CC       derivatives into the 3-oxoadipate pathway. This enzyme converts
CC       maleylacetate and 2-chloromaleylacetate with similar efficiencies. NADH
CC       is preferred to NADPH as the cosubstrate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxoadipate + NAD(+) = H(+) + maleylacetate + NADH;
CC         Xref=Rhea:RHEA:16981, ChEBI:CHEBI:15378, ChEBI:CHEBI:15775,
CC         ChEBI:CHEBI:16468, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.32;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxoadipate + NADP(+) = H(+) + maleylacetate + NADPH;
CC         Xref=Rhea:RHEA:16985, ChEBI:CHEBI:15378, ChEBI:CHEBI:15775,
CC         ChEBI:CHEBI:16468, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.32;
CC   -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoate and by 3-
CC       oxoadipate, and, in a temperature-dependent manner, by manganese.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5.;
CC   -!- PATHWAY: Aromatic compound metabolism; 3-chlorocatechol degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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; U16782; AAC44727.1; -; Genomic_DNA.
DR   EMBL; AY365053; AAR31044.1; -; Genomic_DNA.
DR   EMBL; CP000093; AAZ65769.1; -; Genomic_DNA.
DR   RefSeq; WP_011178391.1; NZ_AY365053.1.
DR   AlphaFoldDB; P94135; -.
DR   SMR; P94135; -.
DR   EnsemblBacteria; AAZ65769; AAZ65769; Reut_D6471.
DR   KEGG; reu:Reut_D6471; -.
DR   HOGENOM; CLU_007207_0_1_4; -.
DR   OMA; GDCLATR; -.
DR   OrthoDB; 1456634at2; -.
DR   UniPathway; UPA00083; -.
DR   GO; GO:0018506; F:maleylacetate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:1901168; P:3-chlorocatechol catabolic process; IDA:CACAO.
DR   CDD; cd08177; MAR; 1.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   InterPro; IPR034786; MAR.
DR   PANTHER; PTHR11496; PTHR11496; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; NAD;
KW   Oxidoreductase; Plasmid.
FT   CHAIN           1..359
FT                   /note="Maleylacetate reductase 2"
FT                   /id="PRO_0000087852"
SQ   SEQUENCE   359 AA;  37504 MW;  FC951B482B2575BF CRC64;
     MTGDLNEFVA HFWPVRVVFG AGSTERIPAE VKRLGARRAL VLCTPDQRDL AQRVLGDLGD
     LGAGFHDGAV MHVPEASVTR AAQAARDADA DLLVAVGGGS TIGLAKALAL HHGMRFVALP
     TTYAGSEMTP IWGLTADGAK RTGRDPRVLP STVLYDPHHL TSLPPEVTGP SGMNAIAHAV
     ESMYAPDRNP ITMLLAEESI RAMAQGLPVA VDSPGDLDAR TRTLYAAWLA GTVLGMVSMG
     LHHKLCHVLG GRFNLPHAPM HAVLLPHVAA FNEVAAPAEL GRVAAALGAP GPGGAGAALH
     ALLRFTCTER SLAAIGMPAQ GIYDAAEHAL ADAYANPRQA SREDIARLLR AAFTGEMPA