Reviewed, UniProtKB/Swiss-Prot P94135 (TFDF2_RALEJ)

Names and origin

Protein names

Recommended name:
    Maleylacetate reductase 2
    EC=1.3.1.32
Alternative name(s):
    Maleylacetate reductase II
    Chloromaleylacetate reductase

Gene names

Name:	tfdFII
Ordered Locus Names:	Reut_D6471

Encoded on

Plasmid pJP4 Ref.1 Ref.2 Ref.4
Plasmid pReut1 Ref.3

Organism

Ralstonia eutropha (strain JMP134) (Alcaligenes eutrophus) [Complete proteome] [HAMAP]

Taxonomic identifier

264198 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a major role in the degradation of chloroaromatic compounds by channeling maleylacetate and some of its substituted derivatives into the 3-oxoadipate pathway. This enzyme converts maleylacetate and 2-chloromaleylacetate with similar efficiencies. NADH is preferred to NADPH as the cosubstrate.
Catalytic activity	3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H.
Enzyme regulation	Inhibited by p-chloromercuribenzoate and by 3-oxoadipate, and, in a temperature-dependent manner, by manganese.
Pathway	Aromatic compound metabolism; 3-chlorocatechol degradation.
Subunit structure	Homodimer Probable.
Sequence similarities	Belongs to the iron-containing alcohol dehydrogenase family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.5.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	maleylacetate reductase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 359	359	Maleylacetate reductase 2		PRO_0000087852

Sequences

	Sequence		Length	Mass (Da)
	P94135-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: FC951B482B2575BF	FASTA	359	37,504
	10 20 30 40 50 60 MTGDLNEFVA HFWPVRVVFG AGSTERIPAE VKRLGARRAL VLCTPDQRDL AQRVLGDLGD 70 80 90 100 110 120 LGAGFHDGAV MHVPEASVTR AAQAARDADA DLLVAVGGGS TIGLAKALAL HHGMRFVALP 130 140 150 160 170 180 TTYAGSEMTP IWGLTADGAK RTGRDPRVLP STVLYDPHHL TSLPPEVTGP SGMNAIAHAV 190 200 210 220 230 240 ESMYAPDRNP ITMLLAEESI RAMAQGLPVA VDSPGDLDAR TRTLYAAWLA GTVLGMVSMG 250 260 270 280 290 300 LHHKLCHVLG GRFNLPHAPM HAVLLPHVAA FNEVAAPAEL GRVAAALGAP GPGGAGAALH 310 320 330 340 350 ALLRFTCTER SLAAIGMPAQ GIYDAAEHAL ADAYANPRQA SREDIARLLR AAFTGEMPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	van der Meer J.R. Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants and evolution of specialized chloroaromatic degradation pathways." Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T., Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B. Environ. Microbiol. 6:655-668(2004) [PubMed: 15186344] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete sequence of plasmid 1 of Ralstonia eutropha JMP134." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134(pJP4)." Seibert V., Stadler-Fritzsche K., Schlomann M. J. Bacteriol. 175:6745-6754(1993) [PubMed: 8226615] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-32, CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U16782 Genomic DNA. Translation: AAC44727.1. AY365053 Genomic DNA. Translation: AAR31044.1. CP000093 Genomic DNA. Translation: AAZ65769.1.
RefSeq	YP_025392.1. YP_293626.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2847409. 3607895.
GenomeReviews	Gene locus Reut_D6471 in contig CP000093_GR.
KEGG	reu:Reut_D6471.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P94135.
Enzyme and pathway databases
BioCyc	REUT264198:REUT_D6471-MON.
Family and domain databases
InterPro	IPR001670. Fe_AlcDHase. [Graphical view]
Pfam	PF00465. Fe-ADH. 1 hit. [Graphical view]
PROSITE	PS00913. ADH_IRON_1. False negative. PS00060. ADH_IRON_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TFDF2_RALEJ

Accession

Primary (citable) accession number: P94135
Secondary accession number(s): Q46M61

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	May 1, 1997
Last modified:	November 25, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)