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Q8GQN9 (BCLA_THAAR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Benzoate--CoA ligase
EC=6.2.1.25
Alternative name(s):
Benzoyl-CoA synthetase
Gene names
Name:bclA
OrganismThauera aromatica
Taxonomic identifier59405 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Thauera

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the ligation of benzoate and CoA to form benzoyl-CoA at the expense of ATP. The enzyme also ligates 2-aminobenzoate and CoA. The enzyme shows activity toward a number of benzoate derivatives. Ref.1

Catalytic activity

ATP + benzoate + CoA = AMP + diphosphate + benzoyl-CoA.

Subunit structure

Monomer. Ref.1

Induction

By benzoate and 2-aminobenzoate. Ref.1

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. Benzoate-CoA ligase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=25 µM for benzoate Ref.1

KM=150 µM for 2-aminobenzoate

KM=370 µM for ATP

KM=160 µM for CoA

Vmax=16.5 µmol/min/mg enzyme with benzoate as substrate

Vmax=9.9 µmol/min/mg enzyme with 2-aminobenzoate as substrate

pH dependence:

Optimum pH is 8.5.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

benzoate-CoA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 527527Benzoate--CoA ligase
PRO_0000350737

Sequences

Sequence LengthMass (Da)Tools
Q8GQN9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 40D7442C7E72109E

FASTA52757,051
        10         20         30         40         50         60 
MYTLSVADHS NTPPAIKIPE RYNAADDLIG RNLLAGRGGK TVYIDDAGSY TYDELALRVN 

        70         80         90        100        110        120 
RCGSALRTTL GLQPKDRVLV CVLDGIDFPT TFLGAIKGGV VPIAINTLLT ESDYEYMLTD 

       130        140        150        160        170        180 
SAARVAVVSQ ELLPLFAPML GKVPTLEHLV VAGGAGEDSL AALLATGSEQ FEAAPTRPDD 

       190        200        210        220        230        240 
HCFWLYSSGS TGAPKGTVHI HSDLIHTAEL YARPILGIRE GDVVFSAAKL FFAYGLGNGL 

       250        260        270        280        290        300 
IFPLAVGATA VLMAERPTPA AVFERLRRHQ PDIFYGVPTL YASMLANPDC PKEGELRLRA 

       310        320        330        340        350        360 
CTSAGEALPE DVGRRWQARF GVDILDGIGS TEMLHIFLSN RAGDVHYGTS GKPVPGYRLR 

       370        380        390        400        410        420 
LIDEDGAEIT TAGVAGELQI SGPSSAVMYW NNPEKTAATF MGEWTRSGDK YLVNDEGYYV 

       430        440        450        460        470        480 
YAGRSDDMLK VSGIYVSPIE VESALIAHEA VLEAAVVGWE DEDHLIKPKA FIVLKPGYGA 

       490        500        510        520 
GEALRTDLKA HVKNLLAPYK YPRWIEFVDD LPKTATGKIQ RFKLRSA

« Hide

References

[1]"Benzoate-coenzyme A ligase from Thauera aromatica: an enzyme acting in anaerobic and aerobic pathways."
Schuehle K., Gescher J., Feil U., Paul M., Jahn M., Schaegger H., Fuchs G.
J. Bacteriol. 185:4920-4929(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-34, FUNCTION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION.
Strain: DSM 6984 / K172.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF373594 Genomic DNA. Translation: AAN32623.1.

3D structure databases

ProteinModelPortalQ8GQN9.
SMRQ8GQN9. Positions 35-526.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3061.

Family and domain databases

InterProIPR000873. AMP-dep_Synth/Lig.
IPR011957. Benz_CoA_lig.
IPR025110. DUF4009.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. DUF4009. 1 hit.
[Graphical view]
TIGRFAMsTIGR02262. benz_CoA_lig. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBCLA_THAAR
AccessionPrimary (citable) accession number: Q8GQN9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: March 1, 2003
Last modified: May 29, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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