ID A0A1B7LFH8_9FIRM Unreviewed; 426 AA.
AC A0A1B7LFH8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 ORFNames=A6M21_08440 {ECO:0000313|EMBL:OAT82915.1};
OS Desulfotomaculum copahuensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=1838280 {ECO:0000313|EMBL:OAT82915.1, ECO:0000313|Proteomes:UP000078532};
RN [1] {ECO:0000313|EMBL:OAT82915.1, ECO:0000313|Proteomes:UP000078532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMa1 {ECO:0000313|EMBL:OAT82915.1,
RC ECO:0000313|Proteomes:UP000078532};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAT82915.1}.
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DR EMBL; LYVF01000127; OAT82915.1; -; Genomic_DNA.
DR RefSeq; WP_066667595.1; NZ_LYVF01000127.1.
DR AlphaFoldDB; A0A1B7LFH8; -.
DR STRING; 1838280.A6M21_08440; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000078532; Unassembled WGS sequence.
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:OAT82915.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000078532}.
FT DOMAIN 80..285
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 334..424
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 426 AA; 47782 MW; 2586E238FFEE9CC9 CRC64;
MAVPARQIDY FDYEALYVQQ AVKLREMLRR VYRNSSFYRK KLDEAGIDPE SIRTMDDLAR
VPFTTKDELR TGYPLGLMAV PEDAVVRIHS SSGTTGKPVI VPYTGRDVEV WAEMMARCLR
MTGVNRRDRV QVTPGYGLWT AGIGFQAGVE RLGAMAVPTG PGNTEKQIEM MLDLHTTVLI
GTSSYGLLLA EEIARRGLQE KVGLRLGIFG SERWGDKMRR RIESTLGIDT FDIYGLTEIY
GPGIGIDCPE HTGIHFWSDH LLFEVIDPHT GAQLPAGEEG ELVITTLSKE GMPLLRYRTR
DISRLISAAC PCGSPYPLME RVLGRTDDRI KIKGVNIYPG QIEDVLKMVA GACSEYQIVL
TRKEAKDYML LKVEGLPEYP PAEVALGCQR TIKSRIGVHC EVEVLPRGSL PRSEKKSRRV
FDRREE
//
