[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=DSM 6984 / K172; DOI=10.1128/JB.182.2.272-277.2000; PubMed=10629170 [NCBI, ExPASy, EBI, Israel, Japan] Leuthner B., Heider J.; "Anaerobic toluene catabolism of Thauera aromatica: the bbs operon codes for enzymes of beta-oxidation of the intermediate benzylsuccinate."; J. Bacteriol. 182:272-277(2000).
[2]	CHARACTERIZATION. STRAIN=DSM 6984 / K172; DOI=10.1007/s00203-002-0484-5; PubMed=12420174 [NCBI, ExPASy, EBI, Israel, Japan] Leutwein C., Heider J.; "(R)-benzylsuccinyl-CoA dehydrogenase of Thauera aromatica, an enzyme of the anaerobic toluene catabolic pathway."; Arch. Microbiol. 178:517-524(2002).

Comments

CATALYTIC ACTIVITY: (R)-2-benzylsuccinyl-CoA + 2 electron-transferring flavoprotein = (E)-2-benzylidenesuccinyl-CoA + 2 reduced electron-transferring flavoprotein.
COFACTOR: FAD.
ENZYME REGULATION: Inhibited by (S)-benzylsuccinyl-CoA.
PATHWAY: Xenobiotic degradation; toluene degradation .
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the acyl-CoA 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

AF173961; AAF89842.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P15651; 1JQI. [HSSP ENTRY / PDB]

ModBase

Q9KJE8.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-687; -.

Family and domain databases

InterPro

IPR006091; Acyl-CoA_DHase/Oxase_M.
IPR006089; Acyl-CoA_DHase_CS.
IPR006092; Acyl-CoA_DHase_N.
IPR006090; Acyl-CoA_Oxase/DHase_1.
IPR013786; AcylCoA_DH/ox_N.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 1.

Pfam

PF00441; Acyl-CoA_dh_1; 1.
PF02770; Acyl-CoA_dh_M; 1.
PF02771; Acyl-CoA_dh_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00072; ACYL_COA_DH_1; FALSE_NEG.
PS00073; ACYL_COA_DH_2; FALSE_NEG.

Other

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

Keywords

Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 406`	`406`		`(R)-benzylsuccinyl-CoA dehydrogenase.`	`PRO_0000201205`

Sequence information

Length: 406 AA [This is the length of the unprocessed precursor]

Molecular weight: 45583 Da [This is the MW of the unprocessed precursor]

CRC64: FC6B7DDC3BD48B11 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDFSLSEEQT MLKEVARRFT ANELMPLEKV LLEREMRMWT DGYTLLPEAD HARLMKITQE 

        70         80         90        100        110        120 
MGFWGIEVDE KLGGQGLGMF AKTLVVEEMS KSLIGFSHHG FTLPPDAPNL YYLEECGSPA 

       130        140        150        160        170        180 
QRDKYVRRYC RGEIDSAMMA TEPGAGSDIS GLTTTAVREN GQWVINGSKI FISKCDKDEL 

       190        200        210        220        230        240 
FFICIAVTDK EAPTKRRFTA FILDKDTPGL RIGAEIPVIG AMPTWSVYLD NVRVGDEAVL 

       250        260        270        280        290        300 
GEVGDAFIPL QNRFGVRRIE LAAHCTGMAE RLIQMMIDQA NLRKTFGVAL ADRQTVQNWI 

       310        320        330        340        350        360 
ADSTIELEQV RLQLYFTAWK SDQGHKDLRL EAASLKIAAT EMLTRVADRA IQLHGGLGLS 

       370        380        390        400 
REMGIEYVAR MVRIWRVVEG ASEIHRMSIA KKLLTDGRTY SPFVAA

Q9KJE8 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