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4-chlorobenzoate--CoA ligase (4-CBA:CoA ligase) (EC 6.2.1.33)

 CBACL_PSEUC             Reviewed;         528 AA.
A5JTM6;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 1.
23-MAY-2018, entry version 29.
RecName: Full=4-chlorobenzoate--CoA ligase {ECO:0000303|PubMed:1610806, ECO:0000303|PubMed:9398293};
Short=4-CBA:CoA ligase {ECO:0000312|EMBL:ABQ44579.1};
EC=6.2.1.33;
Pseudomonas sp. (strain CBS-3).
Bacteria; Proteobacteria.
NCBI_TaxID=72586;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1351742; DOI=10.1021/bi00139a024;
Babbitt P.C., Kenyon G.L., Martin B.M., Charest H., Slyvestre M.,
Scholten J.D., Chang K.H., Liang P.H., Dunaway-Mariano D.;
"Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid
sequence identities among families of acyl:adenyl ligases, enoyl-CoA
hydratases/isomerases, and acyl-CoA thioesterases.";
Biochemistry 31:5594-5604(1992).
[2] {ECO:0000312|EMBL:ABQ44579.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Zhang W., Dunaway-Mariano D.;
"The nucleotide sequence upstream and downstream of 4-CBA-CoA ORFs in
9.5 kb Pseudomonas sp. strain CBS 3 chromosomal DNA.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305}
PROTEIN SEQUENCE OF 1-16, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=1418673;
Loffler F., Muller R., Lingens F.;
"Purification and properties of 4-halobenzoate-coenzyme A ligase from
Pseudomonas sp. CBS3.";
Biol. Chem. Hoppe-Seyler 373:1001-1007(1992).
[4] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
PATHWAY, AND SUBUNIT.
PubMed=1610806; DOI=10.1021/bi00139a025;
Chang K.H., Liang P.H., Beck W., Scholten J.D., Dunaway-Mariano D.;
"Isolation and characterization of the three polypeptide components of
4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3.";
Biochemistry 31:5605-5610(1992).
[5] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF GLY-163; GLY-166; PRO-168; LYS-169 AND GLU-306.
PubMed=9398293; DOI=10.1021/bi971262p;
Chang K.H., Xiang H., Dunaway-Mariano D.;
"Acyl-adenylate motif of the acyl-adenylate/thioester-forming enzyme
superfamily: a site-directed mutagenesis study with the Pseudomonas
sp. strain CBS3 4-chlorobenzoate:coenzyme A ligase.";
Biochemistry 36:15650-15659(1997).
-!- FUNCTION: Catalyzes the formation of chlorobenzoyl-CoA via a 2
step reaction. First 4-chlorobenzoyl is adenylated by ATP,
followed by acyl transfer from the 4-chlorobenzoyl-AMP
intermediate to CoA. Benzoate, 4-bromobenzoate, 4-iodobenzoate and
4-methylbenzoate also act as substrates. Inactive towards 4-
aminobenzoate, 4-hydroxybenzoate, 2-aminobenzoate, 2,3-
dihydroxybenzoate, 4-coumarate and the aliphatic carboxylic acids
palmate, caproate, laurate and butyrate. Negligible activity is
detected when ATP is replaced by UTP, CTP or GTP as cosubstrate.
{ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:9398293}.
-!- CATALYTIC ACTIVITY: 4-chlorobenzoate + CoA + ATP = 4-
chlorobenzoyl-CoA + AMP + diphosphate.
{ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:9398293}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:1418673,
ECO:0000269|PubMed:1610806};
-!- ENZYME REGULATION: Unaffected by 5,5'-dithiobis-(2-nitrobenzoic
acid), 4-chloromercuribenzoate and sodium azide. Inhibited by
Cu(2+), Fe(2+) and Zn(2+). Unaffected by Na(+), K(+) and Li(+).
{ECO:0000269|PubMed:1418673}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8.5 uM for 4-chlorobenzoate {ECO:0000269|PubMed:1418673,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
KM=70 uM for CoA {ECO:0000269|PubMed:1418673,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
KM=104 uM for ATP (with magnesium as cofactor)
{ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:9398293};
KM=43 uM for ATP (with manganese as cofactor)
{ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:9398293};
KM=59 uM for ATP (with cobalt as cofactor)
{ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:9398293};
KM=15 uM for 4-bromobenzoate {ECO:0000269|PubMed:1418673,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
KM=17 uM for 4-iodobenzoate {ECO:0000269|PubMed:1418673,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
KM=700 uM for benzoate {ECO:0000269|PubMed:1418673,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
KM=130 uM for 4-methylbenzoate {ECO:0000269|PubMed:1418673,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
pH dependence:
Optimum pH is 8.4. 85% of activity remains at pH 9.0, 54% of
activity remains at pH 7.0. {ECO:0000269|PubMed:1418673,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
Temperature dependence:
Optimum temperature is 35 degrees Celsius.
{ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:9398293};
-!- PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-
hydroxybenzoate from 4-chlorobenzoate: step 2/3.
{ECO:0000269|PubMed:1610806}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1418673,
ECO:0000269|PubMed:1610806}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; EF569604; ABQ44579.1; -; Genomic_DNA.
ProteinModelPortal; A5JTM6; -.
SMR; A5JTM6; -.
PRIDE; A5JTM6; -.
KEGG; ag:ABQ44579; -.
KO; K14417; -.
BioCyc; MetaCyc:MONOMER-14752; -.
SABIO-RK; A5JTM6; -.
UniPathway; UPA01011; UER01021.
GO; GO:0018861; F:4-chlorobenzoate-CoA ligase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008152; P:metabolic process; IEA:InterPro.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding.
CHAIN 1 528 4-chlorobenzoate--CoA ligase.
/FTId=PRO_0000401169.
NP_BIND 161 169 ATP. {ECO:0000250}.
NP_BIND 300 305 ATP. {ECO:0000250}.
BINDING 409 409 ATP. {ECO:0000250}.
MUTAGEN 163 163 G->I: Significantly inhibits the
adenylation part of the reaction.
{ECO:0000269|PubMed:9398293}.
MUTAGEN 166 166 G->I: Significantly inhibits the
adenylation part of the reaction.
{ECO:0000269|PubMed:9398293}.
MUTAGEN 168 168 P->A: No catalytic activity.
{ECO:0000269|PubMed:9398293}.
MUTAGEN 169 169 K->M: Significantly inhibits the
adenylation part of the reaction.
{ECO:0000269|PubMed:9398293}.
MUTAGEN 306 306 E->Q: Significantly inhibits the
adenylation part of the reaction.
{ECO:0000269|PubMed:9398293}.
SEQUENCE 528 AA; 57151 MW; 94D7A38515629603 CRC64;
MQTVHEMLRR AVSRVPHRWA IVDAARSTFD ICRTGETSRN EGSATARLWP QPARPLAVVS
GNSVEAVIAV LALHRLQAVP ALMNPRLKPA EISELVARGE MARAVVANDA GVMEAIRTRV
PSVCVLALDD LVSGSRVPEV AGKSLPPPPC EPEQAGFVFY TSGTTGLPKG AVIPQRAAES
RVLFMATQAG LRHGSHNVVL GLMPLYHTIG FFAVLVAAMA FDGTYVVVEE FDAGNVLKLI
ERERVTAMFA TPTHLDALTT AVEQAGARLE SLEHVTFAGA TMPDTVLERV NRFIPGEKVN
IYGTTEAMNS LYMRAVRIAG TVMRPGFFSE VRIVRVGGDV DDGCPTVKRA SWRWRRRMRP
FQATLTNLRL LQKSFRKAGT GRAICVRDGS GNIVVLGRVD DMIISGGENI HPSEVERILA
AAPGVAEVVV IGVKDERWGQ SVVACVVLQP GASASAERLD AFCRASALAD FKRPRRYVFL
DELPKSAMNK VLRRQLMQHV SATSSAAVVP APAVKQRTYA PSGRAIAR


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