ID N1UZS1_9MICC Unreviewed; 446 AA.
AC N1UZS1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=D477_009188 {ECO:0000313|EMBL:EMY34570.1};
OS Arthrobacter crystallopoietes BAB-32.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY34570.1, ECO:0000313|Proteomes:UP000010729};
RN [1] {ECO:0000313|EMBL:EMY34570.1, ECO:0000313|Proteomes:UP000010729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-32 {ECO:0000313|EMBL:EMY34570.1,
RC ECO:0000313|Proteomes:UP000010729};
RX PubMed=23833141;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT Revealing Genes for Bioremediation.";
RL Genome Announc. 1:e00452-13(2013).
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:EMY34570.1}.
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DR EMBL; ANPE02000109; EMY34570.1; -; Genomic_DNA.
DR RefSeq; WP_005268685.1; NZ_ANPE02000109.1.
DR AlphaFoldDB; N1UZS1; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000010729; 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:EMY34570.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000010729}.
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..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 49837 MW; 5DCFF47E98D5C636 CRC64;
MSTITGTKAR KSTPAEPEIL DPEERMSRDE LEALQLSRLQ HTVAYAYERV PMYKKKFDEA
GVHPGDLKEL SDLKHFPYTD KEDLRQSYPF GMFAVPQNEV ARIHASSGTT GRATVVGYTK
GDLERWETLF ARSLKASGVK QGWKVHNAYG YGLFTGGLGA HYGAEKLGCT VIPMSGGQTE
KQIQLIQDFE PDAILCTPTY LLTIVDAMER AGLDPAKTSL KVAVLGAEPW TEEMRHELET
KLDIDACDIY GLSEVMGPGV AGECIDYKDG STIWEDHFRP EIIDPLTDDV LRDGEHGELV
FTSLTKEAMP VIRYRTHDLT RLLPGTGRPN MRRIGRITGR SDDMIILRGV NLFPTQIEEI
ALRIPGLSPH FQLEITRPNR MDELTVKIER RDDCTPEVAA AAAKDLQKQI KIHVGSSCRI
DVVEPNSLAR SSGKLRRIYD LRNLNG
//
