4HBCL_RHOPA
ID 4HBCL_RHOPA Reviewed; 539 AA.
AC Q53005; Q6NC06;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=4-hydroxybenzoate--CoA/benzoate--CoA ligase;
DE EC=6.2.1.25;
DE EC=6.2.1.27;
DE AltName: Full=4-hydroxybenzoyl-CoA synthetase;
GN Name=hbaA; OrderedLocusNames=RPA0669;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, BLOCKED N-TERMINUS, AND
RP SUBUNIT.
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=8300518; DOI=10.1128/jb.176.3.634-641.1994;
RA Gibson J., Dispensa M., Fogg G.C., Evans D.T., Harwood C.S.;
RT "4-hydroxybenzoate-coenzyme A ligase from Rhodopseudomonas palustris:
RT purification, gene sequence, and role in anaerobic degradation.";
RL J. Bacteriol. 176:634-641(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
CC -!- FUNCTION: Catalyzes the ligation of 4-hydroxybenzoate, benzoate or
CC cyclohex-1,4-dienecarboxylate and CoA at the expense of ATP. The enzyme
CC shows low activity towards cyclo-2,5-dienecarboxylate, 4-
CC fluorobenzoate, 4-chlorobenzoate and 2-methoxybenzoate.
CC {ECO:0000269|PubMed:8300518}.
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:8300518};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:10132, ChEBI:CHEBI:16150, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369,
CC ChEBI:CHEBI:456215; EC=6.2.1.25;
CC Evidence={ECO:0000269|PubMed:8300518};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=400 uM for benzoate {ECO:0000269|PubMed:8300518};
CC KM=120 uM for 4-hydroxybenzoate {ECO:0000269|PubMed:8300518};
CC KM=90 uM for ATP {ECO:0000269|PubMed:8300518};
CC KM=400 uM for CoA {ECO:0000269|PubMed:8300518};
CC pH dependence:
CC Optimum pH is above 9. {ECO:0000269|PubMed:8300518};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8300518}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC Benzoate-CoA ligase subfamily. {ECO:0000305}.
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DR EMBL; U02033; AAA62604.1; -; Genomic_DNA.
DR EMBL; BX572595; CAE26113.1; -; Genomic_DNA.
DR PIR; A58538; A58538.
DR RefSeq; WP_011156236.1; NC_005296.1.
DR AlphaFoldDB; Q53005; -.
DR SMR; Q53005; -.
DR STRING; 258594.RPA0669; -.
DR PRIDE; Q53005; -.
DR EnsemblBacteria; CAE26113; CAE26113; RPA0669.
DR KEGG; rpa:RPA0669; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_59_10_5; -.
DR OMA; PLRDYNA; -.
DR PhylomeDB; Q53005; -.
DR BioCyc; MetaCyc:MON-17402; -.
DR BioCyc; RPAL258594:TX73_RS03455-MON; -.
DR SABIO-RK; Q53005; -.
DR Proteomes; UP000001426; Chromosome.
DR GO; GO:0018859; F:4-hydroxybenzoate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0018858; F:benzoate-CoA ligase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.300.30; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
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; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..539
FT /note="4-hydroxybenzoate--CoA/benzoate--CoA ligase"
FT /id="PRO_5000144018"
SQ SEQUENCE 539 AA; 58930 MW; A17A290F5F6AF455 CRC64;
MPLRDYNAAV DFVDRNVAEG RGGKIAFIDP QRSLSYGELR DAVARVGPML ARLGVEQENR
IALVLKDTVD FPILFWGAIR AGIVPVLLNT RLTADQYRYL LEDSRSRVVF ASSEFLPVIE
EAAADLPHLR TIIAVGDAPA PTLQLANLLA TEQEGGAPAA TCADDIAYWQ YSSGTTGMPK
GVMHVHSSPR VMAENAGRRI GYREDDVVFS AAKLFFAYGL GNAMFCPMGI GATSVLYPER
PTADSVFDTL RLHQPTLLFA VPTLYAAMLA DPRSRTETLP DRLRLCVSAG EPLPAQVGLN
WRNRFGHDIV NGVGSTEMGH LFLTNLPHAV EYGTSGVPVD GYRLRLVGDR GQDVADDEIG
ELLVSGGSSA AGYWNQRDKT RTTFVGEWTR TGDKYHRRAD GVYTYCGRTD DIFKVSGIWV
SPFEIEQALM SHAKVLEAAV IPAEDTDGLI KPKAFIVLAS RGDIDPGALF DELKEHVKSA
IGPWKYPRWI QIMDDLPKTS SGKLQRYLLR EMTLGGIEAT ESAPSEPALY GRVVAGNGR
