ID F7VAG5_9PROT Unreviewed; 447 AA.
AC F7VAG5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=ATPR_0364 {ECO:0000313|EMBL:GAA07360.1};
OS Acetobacter tropicalis NBRC 101654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=749388 {ECO:0000313|EMBL:GAA07360.1, ECO:0000313|Proteomes:UP000004319};
RN [1] {ECO:0000313|EMBL:GAA07360.1, ECO:0000313|Proteomes:UP000004319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101654 {ECO:0000313|EMBL:GAA07360.1,
RC ECO:0000313|Proteomes:UP000004319};
RX PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126;
RA Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I.,
RA Yakushi T., Matsushita K.;
RT "Increased number of Arginine-based salt bridges contributes to the
RT thermotolerance of thermotolerant acetic acid bacteria, Acetobacter
RT tropicalis SKU1100.";
RL Biochem. Biophys. Res. Commun. 409:120-124(2011).
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:GAA07360.1}.
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DR EMBL; BABS01000006; GAA07360.1; -; Genomic_DNA.
DR RefSeq; WP_006557374.1; NZ_BABS01000006.1.
DR AlphaFoldDB; F7VAG5; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000004319; 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; IPR049623; PA_CoA_lig_proteobact_actino.
DR InterPro; IPR011880; PA_CoA_ligase.
DR NCBIfam; TIGR02155; PA_CoA_ligase; 1.
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:GAA07360.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 14..298
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 345..439
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 447 AA; 49845 MW; 8A522E57D132A9AB CRC64;
MNATVYTPAY PHPEAIHDIA VLSRDELMFI QLERMKWSLR HAYENVALYR NRCIAAGVHP
DDLCSLSDLA RFPTTTKADL RDTYPFGMFA VPQERLARIH GSSGTTGKPI VVGYTHADLD
MWAGIVGRSI RAAGGRPGMK LHNAYGYGLF TGGLGMHLGA ERMGCTVIPM SGGMTERQVQ
LIEDFKPQII TVTPSYMLAL LDEFRRQGLD PRASSIKYGI FGAEPWTNSM REEIEQAFDM
HAVDIYGLSE VVGPGVAQEF IETKDGLHFW EDHFYPEIIN PETGAPVADG EPGELVITSL
SKEAFPIVRY RTRDLTRLLP GTMVPAVRRI EKIMARSDDM IILRGVNIFP TQVEAALLHC
KWCSAHFQIE LTHHGRMDNM TIHVEPRPEA WNPAETSHRS REIIKTIKNT IGVSVQVSVK
EPGMIPRSNG KVTRVIDNRA KASSILA
//
