ID A0A1G7VV43_9BACT Unreviewed; 438 AA.
AC A0A1G7VV43;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=SAMN05216518_1468 {ECO:0000313|EMBL:SDG63441.1};
OS Bacteroidales bacterium KHT7.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1855373 {ECO:0000313|EMBL:SDG63441.1, ECO:0000313|Proteomes:UP000198526};
RN [1] {ECO:0000313|EMBL:SDG63441.1, ECO:0000313|Proteomes:UP000198526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHT7 {ECO:0000313|EMBL:SDG63441.1,
RC ECO:0000313|Proteomes:UP000198526};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNBQ01000046; SDG63441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7VV43; -.
DR STRING; 1855373.SAMN05216518_1468; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000198526; 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:SDG63441.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000198526}.
FT DOMAIN 93..289
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 339..434
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 438 AA; 49957 MW; 8FB763E9F15C1C0D CRC64;
MDVNSEFLHP DKETLSREEI KALQLERLKA TVKHCMNSEF YKKRFEEAGI TPDDIKTLDD
IRKIPFTTKQ DLRDTYPFGM RSVPLEKCVR LHSSSGTTGN PTVILHTQKD LDEWANAVAR
CLWMVGLRPD DVFQNSSGYG MFTGGLGFQY GAERLGMLTV PAAAGNTLRQ IKFITDFGTT
AIHAVPSYVT RIKEVMDELG IDPKKDTKLK LLAIGAEPHS EEQRKKIEKM LGVKAYNSFG
MSEMCGPGVG FECKEQNGLH FWEDYYIVEI VDPETLEPVP DGEIGELVLT TINREAMPLL
RYRTRDLTRV LGYDCPCGRK HIRIDRMKGR SDDMMVLRGV NIFPIQIEKI LMQFKELSTD
YLITLTTDND NDNMTVEVEL DQLFTDDYTR LQSLTKEITR RLKDEILLTP RVKLVPKGTL
PKSEGKAVRV KDLRTVYQ
//
