ID A0A0S7XQ21_9BACT Unreviewed; 437 AA.
AC A0A0S7XQ21;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=AMK68_01255 {ECO:0000313|EMBL:KPJ64592.1};
OS candidate division KD3-62 bacterium DG_56.
OC Bacteria; candidate division KD3-62.
OX NCBI_TaxID=1704032 {ECO:0000313|EMBL:KPJ64592.1, ECO:0000313|Proteomes:UP000052020};
RN [1] {ECO:0000313|EMBL:KPJ64592.1, ECO:0000313|Proteomes:UP000052020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_56 {ECO:0000313|EMBL:KPJ64592.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ64592.1}.
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DR EMBL; LIZY01000018; KPJ64592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7XQ21; -.
DR PATRIC; fig|1704032.3.peg.1169; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000052020; 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:KPJ64592.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 79..285
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 335..431
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 437 AA; 49296 MW; 28C46F30D67DF918 CRC64;
MPVWSKRWEC MDREELQQVQ LERLQATVNR AYKNVRFYHQ QMDAADLAPE DVQSLQDIRR
FPFTTKDDMR EGYPYEMFAV PLREIVRIHA SSGTTGQPTV CGYTKRDLQT WSELVARIMT
AGGVTRNDVV QIFFGYGLFT GAFGHHYGAE EIGASVIPAS AGGTQRQIQL MQDFRTTALV
GTPSYALYIA EVLEEMGIHP DQLSLRVGLF GAEPWSERMR EAIENKLHIT ASDNYGLSEI
IGPGVSGECE HRNGMHISED HFLPEIIDPQ TGELLEPGQE GELVITALTR EAMPMIRFRT
RDLTTLDVEP CPCGRTTARM ARVGQRTDDM IIYRGVNIYP SQVEAILAEV EGTEPHFQIV
LDRKGALDEM EVQVEVSPEI FPDTMRKLVE MEERIRSRLA AQIGISPRIK LVEPKTLERT
SGKAQRVIDR RPDAEGG
//
