ID E6MEZ0_9FIRM Unreviewed; 456 AA.
AC E6MEZ0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
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 Name=paaK {ECO:0000313|EMBL:EFV02340.1};
GN ORFNames=HMP0721_0573 {ECO:0000313|EMBL:EFV02340.1};
OS Pseudoramibacter alactolyticus ATCC 23263.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Pseudoramibacter.
OX NCBI_TaxID=887929 {ECO:0000313|EMBL:EFV02340.1, ECO:0000313|Proteomes:UP000004754};
RN [1] {ECO:0000313|EMBL:EFV02340.1, ECO:0000313|Proteomes:UP000004754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23263 {ECO:0000313|EMBL:EFV02340.1,
RC ECO:0000313|Proteomes:UP000004754};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) 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:EFV02340.1}.
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DR EMBL; AEQN01000010; EFV02340.1; -; Genomic_DNA.
DR AlphaFoldDB; E6MEZ0; -.
DR STRING; 887929.HMP0721_0573; -.
DR eggNOG; COG1541; Bacteria.
DR HOGENOM; CLU_035301_1_1_9; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000004754; 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; IPR011880; PA_CoA_ligase.
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:EFV02340.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000004754}.
FT DOMAIN 101..307
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 357..453
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 456 AA; 50959 MW; 150A3A10BE975C6C CRC64;
MAPPEKVIDF YFWIKKRKRE ALIMIWSTTE TLDRTELRLI QLEKLKKTIR YAYNRVPFYQ
QKFHEANITP DDIQTLDDLK KIPFTTKDDF RDHYPFDLFA VPKEEIIRYH ASSGTTGNPT
VVGYTQNDMA VWKECIARIA AMAGVTYHDT AQIAFGYGLF TGALGLHQGL ETIGASVIPM
SSGNSKKQIK IMKDWGTTAL IATPSYALHL SEVAQSMEID PRTDLKVRYG VLGSEPSTEA
MRAKLNQNWG MQATENYGMS ELGGPGVAGE CLHYHGMHIN EDYFICEIID PATGEVLPEG
EQGELVVTPL FREATPVLRY RTKDITSLDS SPCTCGRTTM RMSKIAGRTD DMLIISGVNV
FPSQIEEVLL SIDGIGSNYL ITISKKGYLD RMDINVEVTD ASLLDSASRL DQLLGTVKTQ
LHTVLGIHPV IHLVEPLSME ASKGKAVRVI DKRNEK
//
