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Benzoate--CoA ligase (EC 6.2.1.25) (Benzoyl-CoA synthetase)

 BCLA_THAAR              Reviewed;         527 AA.
Q8GQN9;
23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
30-AUG-2017, entry version 46.
RecName: Full=Benzoate--CoA ligase;
EC=6.2.1.25;
AltName: Full=Benzoyl-CoA synthetase;
Name=bclA;
Thauera aromatica.
Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
Zoogloeaceae; Thauera.
NCBI_TaxID=59405;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-34, FUNCTION,
SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
INDUCTION.
STRAIN=DSM 6984 / K172;
PubMed=12897012; DOI=10.1128/JB.185.16.4920-4929.2003;
Schuehle K., Gescher J., Feil U., Paul M., Jahn M., Schaegger H.,
Fuchs G.;
"Benzoate-coenzyme A ligase from Thauera aromatica: an enzyme acting
in anaerobic and aerobic pathways.";
J. Bacteriol. 185:4920-4929(2003).
-!- 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. {ECO:0000269|PubMed:12897012}.
-!- CATALYTIC ACTIVITY: ATP + benzoate + CoA = AMP + diphosphate +
benzoyl-CoA.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=25 uM for benzoate {ECO:0000269|PubMed:12897012};
KM=150 uM for 2-aminobenzoate {ECO:0000269|PubMed:12897012};
KM=370 uM for ATP {ECO:0000269|PubMed:12897012};
KM=160 uM for CoA {ECO:0000269|PubMed:12897012};
Vmax=16.5 umol/min/mg enzyme with benzoate as substrate
{ECO:0000269|PubMed:12897012};
Vmax=9.9 umol/min/mg enzyme with 2-aminobenzoate as substrate
{ECO:0000269|PubMed:12897012};
pH dependence:
Optimum pH is 8.5. {ECO:0000269|PubMed:12897012};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12897012}.
-!- INDUCTION: By benzoate and 2-aminobenzoate.
{ECO:0000269|PubMed:12897012}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. Benzoate-CoA ligase subfamily. {ECO:0000305}.
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EMBL; AF373594; AAN32623.1; -; Genomic_DNA.
ProteinModelPortal; Q8GQN9; -.
SMR; Q8GQN9; -.
BioCyc; MetaCyc:MONOMER-3061; -.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0018858; F:benzoate-CoA ligase activity; IEA:UniProtKB-EC.
GO; GO:0008152; P:metabolic process; IEA:InterPro.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR000873; AMP-dep_Synth/Lig.
InterPro; IPR011957; Benz_CoA_lig.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
TIGRFAMs; TIGR02262; benz_CoA_lig; 1.
1: Evidence at protein level;
ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding.
CHAIN 1 527 Benzoate--CoA ligase.
/FTId=PRO_0000350737.
SEQUENCE 527 AA; 57051 MW; 40D7442C7E72109E CRC64;
MYTLSVADHS NTPPAIKIPE RYNAADDLIG RNLLAGRGGK TVYIDDAGSY TYDELALRVN
RCGSALRTTL GLQPKDRVLV CVLDGIDFPT TFLGAIKGGV VPIAINTLLT ESDYEYMLTD
SAARVAVVSQ ELLPLFAPML GKVPTLEHLV VAGGAGEDSL AALLATGSEQ FEAAPTRPDD
HCFWLYSSGS TGAPKGTVHI HSDLIHTAEL YARPILGIRE GDVVFSAAKL FFAYGLGNGL
IFPLAVGATA VLMAERPTPA AVFERLRRHQ PDIFYGVPTL YASMLANPDC PKEGELRLRA
CTSAGEALPE DVGRRWQARF GVDILDGIGS TEMLHIFLSN RAGDVHYGTS GKPVPGYRLR
LIDEDGAEIT TAGVAGELQI SGPSSAVMYW NNPEKTAATF MGEWTRSGDK YLVNDEGYYV
YAGRSDDMLK VSGIYVSPIE VESALIAHEA VLEAAVVGWE DEDHLIKPKA FIVLKPGYGA
GEALRTDLKA HVKNLLAPYK YPRWIEFVDD LPKTATGKIQ RFKLRSA


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