ID A0A1G8MBL8_9RHOB Unreviewed; 436 AA.
AC A0A1G8MBL8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN05421850_104123 {ECO:0000313|EMBL:SDI65313.1};
OS Lutimaribacter saemankumensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Lutimaribacter.
OX NCBI_TaxID=490829 {ECO:0000313|EMBL:SDI65313.1, ECO:0000313|Proteomes:UP000199340};
RN [1] {ECO:0000313|EMBL:SDI65313.1, ECO:0000313|Proteomes:UP000199340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28010 {ECO:0000313|EMBL:SDI65313.1,
RC ECO:0000313|Proteomes:UP000199340};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNEB01000004; SDI65313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8MBL8; -.
DR STRING; 490829.SAMN05421850_104123; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000199340; 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:SDI65313.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000199340}.
FT DOMAIN 97..293
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 339..432
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 436 AA; 48506 MW; 9C110D4953862D4A CRC64;
MEDLSPRPGD LEHIETASRD EISALQLDRM KWSLRHAYYN VPFYRKSFDD AGVHPDDLKS
LSDLSKFPFT VKTDLRDNYP FGMFAVPREE VQRIHASSGT TGQPTVVGYT KNDLDVWGTV
VARSLRASGL RRGDLLHNAY GYGLFTGGLG IHLGADKLGL STVPISGGMT PRQVRLIEDF
RATGITVTPS YALSILDEYA AQGLDPRKSP LKVGIFGAEP WTNAMRREIE EAFDMHAVDI
YGLSEVMGPG VANECVETKD GLHIWEDHFY PEVIDPQTGE VLPDGELGEL VFTSLSKEAF
PIVRYRTRDL TRLLPGTARS MRRMEKVTGR SDDMIILRGV NVFPTQIEEV LMQVRDLAPH
FQIELHRKGR MDAMRVLCEA CEGVGQSGRD AAARDMAHRI KQMVGVSVEI HVSDPGGVER
SQGKAVRIID NRPKGD
//
