ID B0MKI6_9FIRM Unreviewed; 447 AA.
AC B0MKI6;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-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=EUBSIR_00342 {ECO:0000313|EMBL:EDS01801.1};
OS [Eubacterium] siraeum DSM 15702.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=428128 {ECO:0000313|EMBL:EDS01801.1, ECO:0000313|Proteomes:UP000005326};
RN [1] {ECO:0000313|EMBL:EDS01801.1, ECO:0000313|Proteomes:UP000005326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15702 {ECO:0000313|EMBL:EDS01801.1,
RC ECO:0000313|Proteomes:UP000005326};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS01801.1, ECO:0000313|Proteomes:UP000005326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15702 {ECO:0000313|EMBL:EDS01801.1,
RC ECO:0000313|Proteomes:UP000005326};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium siraeum (DSM 15702).";
RL Submitted (NOV-2007) 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:EDS01801.1}.
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DR EMBL; ABCA03000031; EDS01801.1; -; Genomic_DNA.
DR AlphaFoldDB; B0MKI6; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000005326; 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; 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};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 105..300
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 349..445
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 447 AA; 49869 MW; ECD774A894D98F5F CRC64;
MHTPRAKNKK EGYNMSFFQK DIETMPRAEL EKLQLEKLKH ITKYCYDNVP LYKRKFDEAG
FDCTKIKALS DIQYIPYTTK SDFRDNYPFG MFATPLKNVT RLHASSGTTG KPTVVGYTKN
DLDMWSDCVA RLVTAAGATD EDIVQIAFGY GLFTGALGLH YGLEKIGATV VPCSSGNTEK
QVMLMKDFGT TALVATPSYA MRIGEVAEEM GIGRDELKLR LGLFGSEGCT PEMRAQIEDY
LHLLATDNYG MSELMGPGVS GECSLRCGMH FNEDHFLPEI INPETGEVLP EGSKGELVIT
TLSKEAIPVL RYRTKDITSI TYEKCECGRT HARMSKPSGR SDDMLKIRGV NVFPSQIESV
IMTIPQIAPH YQLVVTREGS SDRLEVKCEL VDGSVLESLE SLSNLQKNIR HNLKTVLGID
TKVTLVEPKT IERFEGKAKR VIDLRNK
//
