ID   CBCL1_ARTSP             Reviewed;         522 AA.
AC   P86831; O85077;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=4-chlorobenzoate--CoA ligase {ECO:0000303|PubMed:15068371, ECO:0000312|EMBL:AAC28265.1};
DE            Short=4-CBA:CoA ligase {ECO:0000303|PubMed:15068371};
DE            EC=6.2.1.33;
GN   Name=fcbA1 {ECO:0000312|EMBL:AAC28265.1};
OS   Arthrobacter sp.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1667;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAC28265.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIB 12013 / TM1 {ECO:0000312|EMBL:AAC28265.1};
RX   PubMed=11371537; DOI=10.1128/jb.183.12.3729-3736.2001;
RA   Gartemann K.H., Eichenlaub R.;
RT   "Isolation and characterization of IS1409, an insertion element of 4-
RT   chlorobenzoate-degrading Arthrobacter sp. strain TM1, and development of a
RT   system for transposon mutagenesis.";
RL   J. Bacteriol. 183:3729-3736(2001).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=NCIB 12013 / TM1 {ECO:0000269|PubMed:15068371};
RX   PubMed=15068371; DOI=10.1023/b:biod.0000015614.94615.34;
RA   Zhou L., Marks T.S., Poh R.P., Smith R.J., Chowdhry B.Z., Smith A.R.;
RT   "The purification and characterisation of 4-chlorobenzoate:CoA ligase and
RT   4-chlorobenzoyl CoA dehalogenase from Arthrobacter sp. strain TM-1.";
RL   Biodegradation 15:97-109(2004).
CC   -!- FUNCTION: Catalyzes the formation of chlorobenzoyl-CoA via a 2 step
CC       reaction. First 4-chlorobenzoate is adenylated by ATP, followed by acyl
CC       transfer from the 4-chlorobenzoyl-AMP intermediate to CoA (By
CC       similarity). Benzoate, 4-bromobenzoate, 4-iodobenzoate and 4-
CC       fluorobenzoate also act as substrates. Inactive towards 4-
CC       nitrobenzoate. {ECO:0000250|UniProtKB:A5JTM6,
CC       ECO:0000269|PubMed:15068371}.
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:15068371};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15068371};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.5 uM for 4-chlorobenzoate {ECO:0000269|PubMed:15068371};
CC         KM=30 uM for CoA {ECO:0000269|PubMed:15068371};
CC         KM=238 uM for ATP {ECO:0000269|PubMed:15068371};
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:15068371};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.
CC         {ECO:0000269|PubMed:15068371};
CC   -!- PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-
CC       hydroxybenzoate from 4-chlorobenzoate: step 2/3.
CC       {ECO:0000250|UniProtKB:A5JTM6}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15068371}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000255}.
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DR   EMBL; AF042490; AAC28265.1; -; Genomic_DNA.
DR   AlphaFoldDB; P86831; -.
DR   SMR; P86831; -.
DR   PRIDE; P86831; -.
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; Ligase; Nucleotide-binding.
FT   CHAIN           1..522
FT                   /note="4-chlorobenzoate--CoA ligase"
FT                   /id="PRO_0000402569"
FT   BINDING         161..169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         300..305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         410
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ   SEQUENCE   522 AA;  56687 MW;  FCEB299F55AE47B3 CRC64;
     MRTAFELVAW SAHRQPGAVA LLDPESGHRL TYSELLKRIE GVATVLASRG VVRDELVATA
     MANTLDHAII LLALNRLGAI PVIINPRLKA DEMVQLIRRD NIRTVIRTVA EGKSGTPADI
     DGVEELTLSA EVLSEGLRID GNATPAFEAP RPEDPAFVFY TSGTTGLPKG VVIPHRAIEP
     RVLFMSTQAG LRFGGHNNLL GLMPIHHVIG FFGVFLGSLA FNGTWIPVTA FDPAQAVKWV
     EELDVTCLFA SPTHFDALLA TSEFAPEKLK SVDSVIFAGA AINQSILKRL EKCLQVPIVD
     IYGTTETMNS LFNPDATQER GLRPGYHSRV QFASVSESPS VALPAGVEGE LVVDASADAT
     FTHYLNNPEA TAAKIVDGWY RTGDSGYVDD SGRVILTGRI DDMINTGAEN VHAEEVEQII
     SRHPAVVEAA VVGLPDTRWG EVVTAVVVVS EPLTADLLDQ VCLDSELANF KRPRRYFVVN
     ELPRNAAMKV SRRTLREYLG AHAADQPNPE TGFIQFTIEE SQ