ID H5YGQ8_9BRAD Unreviewed; 443 AA.
AC H5YGQ8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=Bra471DRAFT_02810 {ECO:0000313|EMBL:EHR02063.1};
OS Bradyrhizobium sp. WSM471.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR02063.1};
RN [1] {ECO:0000313|EMBL:EHR02063.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM471 {ECO:0000313|EMBL:EHR02063.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL Submitted (NOV-2011) 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; CM001442; EHR02063.1; -; Genomic_DNA.
DR RefSeq; WP_007607919.1; NZ_CM001442.1.
DR AlphaFoldDB; H5YGQ8; -.
DR HOGENOM; CLU_035301_1_1_5; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000005774; Chromosome.
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:EHR02063.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 94..299
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 346..440
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 443 AA; 49584 MW; EB4F1E154A504FBA CRC64;
MALSRLKEGG NTYRAEMDAH ERASRDEIMA LQAQRLAWSL KHAYDNVPHY RKAFDAAGVH
PSDFRELSDL AKFPFTVKTD LRDNYPFNMF AVPREKLVRV HASSGTTGKP IVVGYTQRDI
DTWSDVMARS IRAAGGRTGM IIHNAYGYGL FTGGLGVHYG AEKLGCTVVP ISGGMTERQV
QLINDFRPDI ITVTPSYMLA ILDEFKRQKL DPRQCSLKVG IFGAEPWTNA MRGEIEDAFD
MDATDIYGLS EVIGPGVAQE CIETKDGLHI WEDHFYPEVI DPDTGVVLPD GEKGELVFTS
LTKEAFPVIR YRTRDLTRLL PGTARPGMRR MEKVTGRSDD MIILRGVNLF PTQIEEVLLA
TDWCGGHFIL ELTREGRMDE LTIIAEARPE SWDGRGLLDH ADRISTHVKN TIGISSNVRV
VAPATLERSL GKAKRLYDKR PKD
//