ID   3HBCL_THAAR             Reviewed;         523 AA.
AC   Q9AJS8;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=3-hydroxybenzoate--CoA/4-hydroxybenzoate--CoA ligase;
DE            EC=6.2.1.27;
DE            EC=6.2.1.37;
DE   AltName: Full=3-hydroxybenzoyl-CoA synthetase;
GN   Name=hcl;
OS   Thauera aromatica.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=59405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND INDUCTION.
RC   STRAIN=DSM 6984 / CIP 107765 / K172;
RX   PubMed=11208796; DOI=10.1128/jb.183.3.968-979.2001;
RA   Laempe D., Jahn M., Breese K., Schaegger H., Fuchs G.;
RT   "Anaerobic metabolism of 3-hydroxybenzoate by the denitrifying bacterium
RT   Thauera aromatica.";
RL   J. Bacteriol. 183:968-979(2001).
CC   -!- FUNCTION: Catalyzes the ligation of 3-hydroxybenzoate or 4-
CC       hydroxybenzoate and CoA at the expense of ATP. The enzyme shows low
CC       activity towards benzoate, 4-aminobenzoate, 3-aminobenzoate, 3-
CC       fluorobenzoate, 4-fluorobenzoate, 3-chlorobenzoate, and 4-
CC       chlorobenzoate. There is no activity with 3,4-dihydroxybenzoate, 2,3-
CC       dihydroxybenzoate, and 2-hydroxybenzoate as substrates.
CC       {ECO:0000269|PubMed:11208796}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxybenzoate + ATP + CoA = 4-hydroxybenzoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:23116, ChEBI:CHEBI:17879,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57356, ChEBI:CHEBI:456215; EC=6.2.1.27;
CC         Evidence={ECO:0000269|PubMed:11208796};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxybenzoate + ATP + CoA = 3-hydroxybenzoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:25070, ChEBI:CHEBI:16193,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57342, ChEBI:CHEBI:456215; EC=6.2.1.37;
CC         Evidence={ECO:0000269|PubMed:11208796};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=60 uM for 3-hydroxybenzoate {ECO:0000269|PubMed:11208796};
CC         KM=65 uM for 4-hydroxybenzoate {ECO:0000269|PubMed:11208796};
CC         Vmax=4.1 umol/min/mg enzyme with 3-hydroxybenzoate as substrate
CC         {ECO:0000269|PubMed:11208796};
CC         Vmax=3.4 umol/min/mg enzyme with 4-hydroxybenzoate as substrate
CC         {ECO:0000269|PubMed:11208796};
CC       pH dependence:
CC         Optimum pH is above 9. {ECO:0000269|PubMed:11208796};
CC   -!- INDUCTION: By 3-hydroxybenzoate. {ECO:0000269|PubMed:11208796}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       Benzoate-CoA ligase subfamily. {ECO:0000305}.
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DR   EMBL; AJ278289; CAC28158.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AJS8; -.
DR   SMR; Q9AJS8; -.
DR   KEGG; ag:CAC28158; -.
DR   BioCyc; MetaCyc:OHBENCOATHAUERA-MON; -.
DR   BRENDA; 6.2.1.27; 6271.
DR   BRENDA; 6.2.1.37; 6271.
DR   SABIO-RK; Q9AJS8; -.
DR   GO; GO:0018859; F:4-hydroxybenzoate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR011957; Benz_CoA_lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02262; benz_CoA_lig; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11208796"
FT   CHAIN           2..523
FT                   /note="3-hydroxybenzoate--CoA/4-hydroxybenzoate--CoA
FT                   ligase"
FT                   /id="PRO_0000350736"
SQ   SEQUENCE   523 AA;  57607 MW;  B1B8D38322D55AFA CRC64;
     MSEQLQPQQS MNAADEIIGR PLAQGLGEQT AMLCAERSIT YRELDAATNR HGNALRAHGV
     GKGDRVLFLM DDSPELVAAY LGTLRIGAVA VALNVRLAPR DVLYVIQDSA CRLLYIDAEF
     LHLYQQIAGE LEQPPQVVVR GDEAPAPAII AFKHFLDGQA ATLESVQVAP DDVAYWLYSS
     GTTGRPKAVM HAHRSVLIAD RLEREYFGIK PGDRVFTTSK MFFGWSLGHS LMGGLQCGAT
     VIVAPGWPDA ERVMATAARH RPTILFSTPV MYRNLLREGA GESAAMRDIR HFVSAGEKLP
     ENIGQQWLDT FGIPITEGIG ASETVFLFLC ARPDAYRIGS CGKRVPWAEV RLLDELGNEI
     TTPDTPGLIA IRMASQFVGY WKLPETTEKA LRDGWYYPGD MFSFDADGFW YHNGRADDML
     KISGQWVSPG EIESCASAVP GIAEAVVVAV PNDDGLTRLT LFIVPEDPSA SQQKLSEAWM
     TTLRGTLSIY KCPRTIQFLE ELPRTATGKV QKYRLRDMLQ ATL