ID A0A0S8H602_9BACT Unreviewed; 442 AA.
AC A0A0S8H602;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-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=AMJ81_11665 {ECO:0000313|EMBL:KPK80648.1};
OS Phycisphaerae bacterium SM23_33.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703412 {ECO:0000313|EMBL:KPK80648.1, ECO:0000313|Proteomes:UP000054531};
RN [1] {ECO:0000313|EMBL:KPK80648.1, ECO:0000313|Proteomes:UP000054531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_33 {ECO:0000313|EMBL:KPK80648.1};
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:KPK80648.1}.
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DR EMBL; LJUF01000214; KPK80648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8H602; -.
DR PATRIC; fig|1703412.3.peg.1946; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000054531; 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:KPK80648.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 94..290
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 340..436
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 442 AA; 49005 MW; 22C9C2A64F052559 CRC64;
MSAFAFENRI WDEAETTPRD RLGKLQARRL RELVARVAEV PFYKEALARA KVKPGDIKGP
DDIRRLPFTA KEDLRQHYPL GFLAVPRSQV ARFHGSSGTT GKPTFVAYTA DDLELWANLC
ARFLVAGGLR PEHTVQIAFG YGLFTGGFGL HYGVEKVGAS VVPAAAGNTP RQLMLMQDLQ
ADVLVCTPSY ALNIAEVARQ QGIDPRTLPL KFAHFGAEPW TEDMRKQIEA ELDLIASNNY
GLSEVIGPGV SGECAARNGM HISEDHFLAE CVHPDTLEPV ARGEQGELVF TTLTKQAMPL
IRYRTRDIAS LDSSPCPCGR TGARMSWVLG RTDDMLIIRG VNVFPSQIEE ALLRVEGTAP
HYLIEVDRPG AMDEVTVHVE VRPESFSDKM SQMQVLRDRI DREIQAVTGI RANVQLVEPQ
SLERSVGKAK RVVDHRREKG LI
//
