CBACL_PSEUC
ID CBACL_PSEUC Reviewed; 528 AA.
AC A5JTM6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=4-chlorobenzoate--CoA ligase {ECO:0000303|PubMed:1610806, ECO:0000303|PubMed:9398293};
DE Short=4-CBA:CoA ligase {ECO:0000312|EMBL:ABQ44579.1};
DE EC=6.2.1.33;
OS Pseudomonas sp. (strain CBS-3).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=72586;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1351742; DOI=10.1021/bi00139a024;
RA Babbitt P.C., Kenyon G.L., Martin B.M., Charest H., Slyvestre M.,
RA Scholten J.D., Chang K.H., Liang P.H., Dunaway-Mariano D.;
RT "Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid
RT sequence identities among families of acyl:adenyl ligases, enoyl-CoA
RT hydratases/isomerases, and acyl-CoA thioesterases.";
RL Biochemistry 31:5594-5604(1992).
RN [2] {ECO:0000312|EMBL:ABQ44579.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhang W., Dunaway-Mariano D.;
RT "The nucleotide sequence upstream and downstream of 4-CBA-CoA ORFs in 9.5
RT kb Pseudomonas sp. strain CBS 3 chromosomal DNA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-16, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=1418673; DOI=10.1515/bchm3.1992.373.2.1001;
RA Loffler F., Muller R., Lingens F.;
RT "Purification and properties of 4-halobenzoate-coenzyme A ligase from
RT Pseudomonas sp. CBS3.";
RL Biol. Chem. Hoppe-Seyler 373:1001-1007(1992).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND SUBUNIT.
RX PubMed=1610806; DOI=10.1021/bi00139a025;
RA Chang K.H., Liang P.H., Beck W., Scholten J.D., Dunaway-Mariano D.;
RT "Isolation and characterization of the three polypeptide components of 4-
RT chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3.";
RL Biochemistry 31:5605-5610(1992).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF GLY-163; GLY-166; PRO-168; LYS-169 AND GLU-306.
RX PubMed=9398293; DOI=10.1021/bi971262p;
RA Chang K.H., Xiang H., Dunaway-Mariano D.;
RT "Acyl-adenylate motif of the acyl-adenylate/thioester-forming enzyme
RT superfamily: a site-directed mutagenesis study with the Pseudomonas sp.
RT strain CBS3 4-chlorobenzoate:coenzyme A ligase.";
RL Biochemistry 36:15650-15659(1997).
CC -!- FUNCTION: Catalyzes the formation of chlorobenzoyl-CoA via a 2 step
CC reaction. First 4-chlorobenzoyl is adenylated by ATP, followed by acyl
CC transfer from the 4-chlorobenzoyl-AMP intermediate to CoA. Benzoate, 4-
CC bromobenzoate, 4-iodobenzoate and 4-methylbenzoate also act as
CC substrates. Inactive towards 4-aminobenzoate, 4-hydroxybenzoate, 2-
CC aminobenzoate, 2,3-dihydroxybenzoate, 4-coumarate and the aliphatic
CC carboxylic acids palmate, caproate, laurate and butyrate. Negligible
CC activity is detected when ATP is replaced by UTP, CTP or GTP as
CC cosubstrate. {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:9398293}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-chlorobenzoate + ATP + CoA = 4-chlorobenzoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:23220, ChEBI:CHEBI:17861,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57354, ChEBI:CHEBI:456215; EC=6.2.1.33;
CC Evidence={ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:9398293};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806};
CC -!- ACTIVITY REGULATION: Unaffected by 5,5'-dithiobis-(2-nitrobenzoic
CC acid), 4-chloromercuribenzoate and sodium azide. Inhibited by Cu(2+),
CC Fe(2+) and Zn(2+). Unaffected by Na(+), K(+) and Li(+).
CC {ECO:0000269|PubMed:1418673}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.5 uM for 4-chlorobenzoate {ECO:0000269|PubMed:1418673,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
CC KM=70 uM for CoA {ECO:0000269|PubMed:1418673,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
CC KM=104 uM for ATP (with magnesium as cofactor)
CC {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:9398293};
CC KM=43 uM for ATP (with manganese as cofactor)
CC {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:9398293};
CC KM=59 uM for ATP (with cobalt as cofactor)
CC {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:9398293};
CC KM=15 uM for 4-bromobenzoate {ECO:0000269|PubMed:1418673,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
CC KM=17 uM for 4-iodobenzoate {ECO:0000269|PubMed:1418673,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
CC KM=700 uM for benzoate {ECO:0000269|PubMed:1418673,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
CC KM=130 uM for 4-methylbenzoate {ECO:0000269|PubMed:1418673,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
CC pH dependence:
CC Optimum pH is 8.4. 85% of activity remains at pH 9.0, 54% of activity
CC remains at pH 7.0. {ECO:0000269|PubMed:1418673,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9398293};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:1418673, ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:9398293};
CC -!- PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-
CC hydroxybenzoate from 4-chlorobenzoate: step 2/3.
CC {ECO:0000269|PubMed:1610806}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1418673,
CC ECO:0000269|PubMed:1610806}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000255}.
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DR EMBL; EF569604; ABQ44579.1; -; Genomic_DNA.
DR AlphaFoldDB; A5JTM6; -.
DR SMR; A5JTM6; -.
DR PRIDE; A5JTM6; -.
DR KEGG; ag:ABQ44579; -.
DR BioCyc; MetaCyc:MON-14752; -.
DR SABIO-RK; A5JTM6; -.
DR UniPathway; UPA01011; UER01021.
DR GO; GO:0018861; F:4-chlorobenzoate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding.
FT CHAIN 1..528
FT /note="4-chlorobenzoate--CoA ligase"
FT /id="PRO_0000401169"
FT BINDING 161..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 300..305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 163
FT /note="G->I: Significantly inhibits the adenylation part of
FT the reaction."
FT /evidence="ECO:0000269|PubMed:9398293"
FT MUTAGEN 166
FT /note="G->I: Significantly inhibits the adenylation part of
FT the reaction."
FT /evidence="ECO:0000269|PubMed:9398293"
FT MUTAGEN 168
FT /note="P->A: No catalytic activity."
FT /evidence="ECO:0000269|PubMed:9398293"
FT MUTAGEN 169
FT /note="K->M: Significantly inhibits the adenylation part of
FT the reaction."
FT /evidence="ECO:0000269|PubMed:9398293"
FT MUTAGEN 306
FT /note="E->Q: Significantly inhibits the adenylation part of
FT the reaction."
FT /evidence="ECO:0000269|PubMed:9398293"
SQ 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
