[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=1CP; PubMed=9657989 [NCBI, ExPASy, EBI, Israel, Japan] Seibert V., Kourbatova E.M., Golovleva L.A., Schloemann M.; "Characterization of a maleylacetate reductase encoding region from Rhodococcus opacus 1CP."; J. Bacteriol. 180:3503-3508(1998).

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.
CATALYTIC ACTIVITY: 3-oxoadipate + NAD(P)⁺ = 2-maleylacetate + NAD(P)H.
PATHWAY: Aromatic compound metabolism; 3-chlorocatechol degradation .
SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF030176; AAC38802.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

O84992.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13024; -.

Ontologies

GO:0018506;	Molecular function: maleylacetate reductase activity (inferred from electronic annotation from EC).
GO:0046872;	Molecular function: metal ion binding (inferred from electronic annotation from InterPro).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001670; Fe_AlcDHase.
Graphical view of domain structure.

Pfam

PF00465; Fe-ADH; 1.
Pfam graphical view of domain structure.

PROSITE

PS00913; ADH_IRON_1; FALSE_NEG.
PS00060; ADH_IRON_2; FALSE_NEG.

Other

ProtoNet

O84992.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 357`	`357`		`Maleylacetate reductase 1.`	`PRO_0000087847`

Sequence information

Length: 357 AA [This is the length of the unprocessed precursor]

Molecular weight: 37798 Da [This is the MW of the unprocessed precursor]

CRC64: 05BEFE211A7249CF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAERSSEFVF TGNPARVIFG AGRMRNVREE VERLGRGRVL LLGSENLREV CDQVQDLLGE 

        70         80         90        100        110        120 
LFVNRYDGAA MHTPVEVTDI ALAQLRTSEA DCVVAIGGGS TTGLAKALAA RTGVDQVILP 

       130        140        150        160        170        180 
TTYAGSEVTP VLGETVEGRK TTRSTLAVLP ETVIYDVELS KNLPVPIAVA SAVNALAHAV 

       190        200        210        220        230        240 
EAMYSPDANP VVDTWALEAA QALARGLRGL VSDPSCRRIR TDLLRGSWLA GMCLGSVGMA 

       250        260        270        280        290        300 
VHHKLCHTLG GAFGLPHAPT HTVVLPYAMS FNASEVPDVM DSLASAMNVS NAPAGVWDLI 

       310        320        330        340        350 
ADAGGPTSLA SLGLLQTDLD RAADLATEAP YRNPRQITRS GIRDLLQSAW EGNRPPE

O84992 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools