ID A0A1N6MR95_9GAMM Unreviewed; 447 AA.
AC A0A1N6MR95;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 Name=paaK {ECO:0000313|EMBL:SIP71356.1};
GN ORFNames=XIS1_1120060 {ECO:0000313|EMBL:SIP71356.1};
OS Xenorhabdus innexi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=290109 {ECO:0000313|EMBL:SIP71356.1, ECO:0000313|Proteomes:UP000196435};
RN [1] {ECO:0000313|Proteomes:UP000196435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB1681 (deposited as PTA-6826 in the American Type Culture
RC Collection) {ECO:0000313|Proteomes:UP000196435};
RA Gaudriault S.;
RL Submitted (DEC-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FTLG01000016; SIP71356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6MR95; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000196435; 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; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR PANTHER; PTHR43439:SF1; PHENYLACETATE-COENZYME A LIGASE; 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:SIP71356.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000196435}.
FT DOMAIN 94..302
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 349..444
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 447 AA; 50711 MW; F8EA4C27B33E090F CRC64;
MSNNVQHLHS RFTPHAEASH DSIEFASRDK IQAWQFEQMK WTLHHAYNNV PMYRRKFDAI
GIHPGDFRQL EDIAKFPYTT KQDLRDNYPF DTFAVPMEKI VRIHASSGTT GRPTVVGYTQ
QDIDNWAELV ARSLRFAGVT AKDKIHVAYG YGLFTGGLGA HYGAERLGAA VIPMSGGQTE
KQVQLIRDFQ PDVIMMTPSY CLTLLDELER QMEGDARQCS VRVGIFGAEP WTEGLRQEIE
NRMGIKALDI YGLSEIMGPG VAMESLEYAD GSTIWEDHFY PEVIDPDNLN ILPDGGSGEL
VFTTLTKEAM PMIRYRTRDL TRLLPGTARN MRRMGKITGR SDDMLIIRGI NVFPSQVEEQ
ITRFSELSPH YQLEVNRVGN YDSLSVKVEL KDPTQFSIQQ RCSICHKLRH HIKAMIGIST
EVSIVNCGDI PRSEGKAVRV IDRRQQK
//
