ID V6M536_9BACL Unreviewed; 442 AA.
AC V6M536;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, 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=T458_23365 {ECO:0000313|EMBL:EST53706.1};
OS Brevibacillus panacihumi W25.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1408254 {ECO:0000313|EMBL:EST53706.1, ECO:0000313|Proteomes:UP000017973};
RN [1] {ECO:0000313|EMBL:EST53706.1, ECO:0000313|Proteomes:UP000017973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W25 {ECO:0000313|EMBL:EST53706.1,
RC ECO:0000313|Proteomes:UP000017973};
RX PubMed=24459276;
RA Wang X., Jin D., Zhou L., Wu L., An W., Chen Y., Zhao L.;
RT "Draft Genome Sequence of Brevibacillus panacihumi Strain W25, a
RT Halotolerant Hydrocarbon-Degrading Bacterium.";
RL Genome Announc. 2:e01215-13(2014).
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:EST53706.1}.
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DR EMBL; AYJU01000017; EST53706.1; -; Genomic_DNA.
DR RefSeq; WP_023558466.1; NZ_KI629785.1.
DR AlphaFoldDB; V6M536; -.
DR STRING; 1408254.T458_23365; -.
DR PATRIC; fig|1408254.3.peg.4591; -.
DR eggNOG; COG1541; Bacteria.
DR HOGENOM; CLU_035301_1_1_9; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000017973; 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:EST53706.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000017973}.
FT DOMAIN 60..286
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 335..435
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 442 AA; 49159 MW; E0A848088BAFD500 CRC64;
MIFNLEMETL SKDKMERLQL ERLQETVKRV YERVPFHKKA MDAAGVKPDD IQTIEDIRKL
PFMKKTDLRE NYPFNLFAVE MSEVARIHGS SGTKGKPTVV GYTKKDLENW AEIVARAICC
AGGQPGDIFH NAYGYGLFTG GLGLHNGIER MGAVAVPVSG GNTPRQITLI EDFQPRGIAA
TPSYVLNIVE EMKKQGIDPR ATSIKYGIFG AEPWSEEMRV QLEEALDIKA VDIYGLSEVM
GPGVSIECHE AQDGLHIAED HFYAEIIDPV TGDVLPYGQE GELVFTSLTK EAFPVIRYRT
GDIASLNPEP CKCGRTTMRM SRIKGRVDDM LIIRGVNVFP TEIESVLLTF NQLAPQYQVV
IERDGALDRF EVHCELTQEY ASKIGSHDPA ALAPLVKEIS HMIKCTLGVT VVLRVLPPNS
LMRSEGKAIR IVDNRNKPQP AI
//
