ID V2U901_9GAMM Unreviewed; 429 AA.
AC V2U901;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=P255_01357 {ECO:0000313|EMBL:ESK50858.1};
OS Acinetobacter brisouii CIP 110357.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1341683 {ECO:0000313|EMBL:ESK50858.1, ECO:0000313|Proteomes:UP000018418};
RN [1] {ECO:0000313|EMBL:ESK50858.1, ECO:0000313|Proteomes:UP000018418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110357 {ECO:0000313|EMBL:ESK50858.1,
RC ECO:0000313|Proteomes:UP000018418};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter brisouii CIP 110357.";
RL Submitted (OCT-2013) 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 -!- 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:ESK50858.1}.
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DR EMBL; AYEU01000006; ESK50858.1; -; Genomic_DNA.
DR RefSeq; WP_004904948.1; NZ_KI530762.1.
DR AlphaFoldDB; V2U901; -.
DR STRING; 396323.VH98_11255; -.
DR PATRIC; fig|1341683.3.peg.1343; -.
DR HOGENOM; CLU_035301_1_1_6; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000018418; 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:ESK50858.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000018418}.
FT DOMAIN 80..287
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 334..426
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 429 AA; 48323 MW; 3CA02984C64368A5 CRC64;
MQVQDTDIHE NLPLEALRQL QFERLKQTLH HAYQNSAVYR RKFDAAGVHP DDLHTLADLA
KFPFTTKQDL RENYPFGMFA VPKQDIVRLH ASSGTTGKPT VVGYTQQDIH TWADLVARCL
RVAGLDHSDT VQVAYGYGLF TGGLGAHYGV ERLGATVIPM SGGQTEKQIQ LIQDFQPTAL
MVTPSYCVNI IEQLEKQYGT AKETSLKVGI FGAEPWTEEM RREIETRLNI KALDIYGLSE
VMGPGVAMQA ADDNTGLTIW EDHFYPEIIH PETGEVLPDG EMGELVFTTI TKQGMPVIRY
RTRDLTCLMQ GQHCAMRRMQ KVVGRSDDML IIRGVNVFPT QIEEQILKIP QLIPNYEIHV
SKKGYMDTLH IRTEMSQYTQ TAALQLAQEL QHKIKTMVGV SVTVEILAET MLPRSEGKAK
RVIDLRKIA
//
