ID A4XLB2_CALS8 Unreviewed; 415 AA.
AC A4XLB2;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Phenylacetate-coenzyme A ligase {ECO:0000256|PIRNR:PIRNR006444};
DE EC=6.2.1.30 {ECO:0000256|PIRNR:PIRNR006444};
DE AltName: Full=Phenylacetyl-CoA ligase {ECO:0000256|PIRNR:PIRNR006444};
GN OrderedLocusNames=Csac_2114 {ECO:0000313|EMBL:ABP67697.1};
OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS 6331).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP67697.1, ECO:0000313|Proteomes:UP000000256};
RN [1] {ECO:0000313|Proteomes:UP000000256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331
RC {ECO:0000313|Proteomes:UP000000256};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA Kengen S.M.W., Richardson P.;
RT "Genome sequence of the thermophilic hydrogen-producing bacterium
RT Caldicellulosiruptor saccharolyticus DSM 8903.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP67697.1, ECO:0000313|Proteomes:UP000000256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331
RC {ECO:0000313|Proteomes:UP000000256};
RX PubMed=18776029; DOI=10.1128/AEM.00968-08;
RA van de Werken H.J., Verhaart M.R., VanFossen A.L., Willquist K.,
RA Lewis D.L., Nichols J.D., Goorissen H.P., Mongodin E.F., Nelson K.E.,
RA van Niel E.W., Stams A.J., Ward D.E., de Vos W.M., van der Oost J.,
RA Kelly R.M., Kengen S.W.;
RT "Hydrogenomics of the extremely thermophilic bacterium Caldicellulosiruptor
RT saccharolyticus.";
RL Appl. Environ. Microbiol. 74:6720-6729(2008).
CC -!- FUNCTION: Catalyzes the activation of phenylacetic acid (PA) to
CC phenylacetyl-CoA (PA-CoA). {ECO:0000256|PIRNR:PIRNR006444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylacetate + ATP + CoA = AMP + diphosphate +
CC phenylacetyl-CoA; Xref=Rhea:RHEA:20956, ChEBI:CHEBI:18401,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57390, ChEBI:CHEBI:456215; EC=6.2.1.30;
CC Evidence={ECO:0000256|PIRNR:PIRNR006444};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC {ECO:0000256|PIRNR:PIRNR006444}.
CC -!- SIMILARITY: Belongs to the phenylacetyl-CoA ligase family.
CC {ECO:0000256|PIRNR:PIRNR006444}.
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DR EMBL; CP000679; ABP67697.1; -; Genomic_DNA.
DR RefSeq; WP_011917628.1; NC_009437.1.
DR AlphaFoldDB; A4XLB2; -.
DR STRING; 351627.Csac_2114; -.
DR KEGG; csc:Csac_2114; -.
DR eggNOG; COG1541; Bacteria.
DR HOGENOM; CLU_035301_1_1_9; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000000256; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0047475; F:phenylacetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0010124; P:phenylacetate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05913; PaaK; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR028154; AMP-dep_Lig_C.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR011880; PA_CoA_ligase.
DR PANTHER; PTHR43845; BLR5969 PROTEIN; 1.
DR PANTHER; PTHR43845:SF1; BLR5969 PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF14535; AMP-binding_C_2; 1.
DR PIRSF; PIRSF006444; PaaK; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|PIRNR:PIRNR006444, ECO:0000313|EMBL:ABP67697.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 66..275
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 324..414
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 415 AA; 47454 MW; 4651FA592638FFCB CRC64;
MDRVEMREVK EELFLQQIKN AYENSPFYRR KYQELGIDVD DIKHLADIKK LPFTTKEELR
EAYPLGLAST DERKIVRIHS SSGTTGVPVI IPYTQKDIDD WKEMMKRCYQ FAGVTELDRV
QITPAYGLWT AGIGFQLGAE YLGAMVIPMG PGNTEKQLQM MMDLKSTVLV ATSSYGLLLA
EEVIKKGLKD KIHLRVGIFG SERWGEKQRR IIEEYLGIET FDIYGLTEIY GPGIAIDCKY
HDGLHYFDDY LYFEVIDPQT GQDVPDGEFG ELVITTLQKE GAPLIRYRTR DITRKLPGMC
QCGSTYPRID RIVGRTDDMV KVKGVNIFPA QIDTFLKDIK GVGSEYQVVI ERIGFRDKLT
LKVEVEDEFC TSSMKDLISN EFKNKIGVSA EIILCRIGEL PRSEKKTKRI FDLRG
//
