ID A0A1H1EP71_9MICC Unreviewed; 446 AA.
AC A0A1H1EP71;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN04489742_3020 {ECO:0000313|EMBL:SDQ90358.1};
OS Arthrobacter crystallopoietes.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=37928 {ECO:0000313|EMBL:SDQ90358.1, ECO:0000313|Proteomes:UP000181917};
RN [1] {ECO:0000313|EMBL:SDQ90358.1, ECO:0000313|Proteomes:UP000181917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20117 {ECO:0000313|EMBL:SDQ90358.1,
RC ECO:0000313|Proteomes:UP000181917};
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; FNKH01000002; SDQ90358.1; -; Genomic_DNA.
DR RefSeq; WP_074701148.1; NZ_FNKH01000002.1.
DR AlphaFoldDB; A0A1H1EP71; -.
DR STRING; 37928.SAMN04489742_3020; -.
DR KEGG; acry:AC20117_02375; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000181917; 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:SDQ90358.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000181917}.
FT DOMAIN 94..302
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 349..442
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 49848 MW; 63E276775BF6C34B CRC64;
MTTTTGTKAR KSTPAEPETL DPEELMSRDE LEALQLARLQ HTVAYAYERV PMYKKKFDDA
GVRPEDLKEL ADLAKFPYTD KEDLRQSYPF GMFAVPQNEV ARIHASSGTT GRATVVGYTK
GDLERWETLF ARSLRASGVK KGWKVHNAYG YGLFTGGLGA HYGAEKLGCT VIPMSGGQTE
KQIQLIQDFE PDAILCTPTY LLTIVDAMER KGLDPRKTSL KVAVLGAEPW TEEMRHELET
KLDIDACDIY GLSEVMGPGV AGECVDYKDG STIWEDHFRP EIIDPSTDEV LADGEHGELV
FTSLTKEAMP VIRYRTHDLT RLLPGTGRAN MRRIGRITGR SDDMIILRGV NLFPTQIEEI
ALRIPGLSPH FQLEITRPDR MDELTVKIER RDDCTAETAA AAAKDLQKQI KIHVGSSCRI
DIVEPGSLER SNGKLRRIYD LRKSES
//
