Reviewed, UniProtKB/Swiss-Prot Q93T12 (TFDF_DELAC)

Names and origin

Protein names

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

Gene names

Name:

tfdF

Organism

Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans)

Taxonomic identifier

80866 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Delftia

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	3-oxoadipate + NAD(P)+ = 2-maleylacetate + NAD(P)H. UniProtKB P27101
Pathway	Aromatic compound metabolism; 3-chlorocatechol degradation.
Subunit structure	Homodimer Probable. UniProtKB P94135
Sequence similarities	Belongs to the iron-containing alcohol dehydrogenase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
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 – 352	352	Maleylacetate reductase		PRO_0000087850

Sequences

	Sequence		Length	Mass (Da)
	Q93T12-1 [UniParc]. Last modified June 1, 2002. Version 2. Checksum: C72A9D2671FFFAB3	FASTA	352	37,499
	10 20 30 40 50 60 MNFIHDPLTP RVLFGAGRLQ SLGEELKLLG IRRVLVISTP EQRELANQVA ALIPGSVAGF 70 80 90 100 110 120 FDRATMHVPS QIVDQAASVA RELGVDSYVA PGGGSTIGLA KMLALHSSLP IVAIPTTYAG 130 140 150 160 170 180 SEMTSIYGVT ENELKKTGRD RRVLARTVIY DPELTFGLPT GISVTSGLNA IAHAVEGLYA 190 200 210 220 230 240 PEVNPILAIM AQQGIAALAK SIPTIRSAPT DLEARSQAQY GAWLCGSVLG NVSMALHHKL 250 260 270 280 290 300 CHTLGGTFNL PHAETHTVVL PHALAYNTPA IPRANAWLQE ALATREPAQA LFDLAKSNGA 310 320 330 340 350 PVSLQSIGMK EADLDRACEL VMSAQYPNPR PLEKHAIANL LRRAYLGEPP QP

References

[1]	"A transposon encoding the complete 2,4-dichlorophenoxyacetic acid degradation pathway in the alkalitolerant strain Delftia acidovorans P4a." Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W. Microbiology 149:2545-2556(2003) [PubMed: 12949179] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: P4a.
[2]	"Development and application of PCR primers for the detection of the tfd genes in Delftia acidovorans P4a involved in the degradation of 2,4-D." Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W. Acta Biotechnol. 21:321-331(2001) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-235. Strain: P4a.
[3]	"Regulation of catabolic enzymes during long-term exposure of Delftia acidovorans MC1 to chlorophenoxy herbicides." Benndorf D., Davidson I., Babel W. Microbiology 150:1005-1014(2004) [PubMed: 15073309] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15. Strain: MC1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY078159 Genomic DNA. Translation: AAK57010.2.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.3.1.32. 140899.
Family and domain databases
InterPro	IPR001670. ADH_Fe. IPR018211. ADH_Fe_CS. [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

TFDF_DELAC

Accession

Primary (citable) accession number: Q93T12

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 16, 2004
Last sequence update:	June 1, 2002
Last modified:	June 16, 2009
This is version 36 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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