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Database: UniProt
Entry: A0A075KNM3_9FIRM
LinkDB: A0A075KNM3_9FIRM
Original site: A0A075KNM3_9FIRM 
ID   A0A075KNM3_9FIRM        Unreviewed;       432 AA.
AC   A0A075KNM3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=UFO1_4280 {ECO:0000313|EMBL:AIF53823.1};
OS   Pelosinus sp. UFO1.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF53823.1, ECO:0000313|Proteomes:UP000027983};
RN   [1] {ECO:0000313|EMBL:AIF53823.1, ECO:0000313|Proteomes:UP000027983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UFO1 {ECO:0000313|EMBL:AIF53823.1};
RX   PubMed=25189589;
RA   Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L.,
RA   Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.;
RT   "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using
RT   Single-Molecule Real-Time DNA Sequencing Technology.";
RL   Genome Announc. 2:e00881-14(2014).
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; CP008852; AIF53823.1; -; Genomic_DNA.
DR   RefSeq; WP_038674038.1; NZ_CP008852.1.
DR   AlphaFoldDB; A0A075KNM3; -.
DR   STRING; 484770.UFO1_4280; -.
DR   KEGG; puf:UFO1_4280; -.
DR   eggNOG; COG1541; Bacteria.
DR   HOGENOM; CLU_035301_1_1_9; -.
DR   OrthoDB; 580775at2; -.
DR   UniPathway; UPA00930; -.
DR   Proteomes; UP000027983; 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; 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, ECO:0000313|EMBL:AIF53823.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027983}.
FT   DOMAIN          77..284
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          334..430
FT                   /note="AMP-dependent ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14535"
SQ   SEQUENCE   432 AA;  47942 MW;  7493D8174219C043 CRC64;
     MYWNKTIETM EHDQMQQLQA RRLRDVVEHM YQKVPFYRAL MQQEGLLPQD IATLADISKL
     PFMTKQDMRD NYPYGLFAVP PSEIVRIHAS SGTTGKATVV GYTKRDLGMW SEVMARSLTA
     AGVSKQSFVQ ISYGYGLFTG GLGLHYGAEL VGASVIPVSS GNTARQISLM KDFGTTALAC
     TPSYALHLAE TMNEMGIDPK STALKVGILG AEPWSDKMRS QIETSLNIRA TDIYGLSEII
     GPGVACECSE QQGLHINEDH FYPEIIDPLT GEVLADGQKG ELVLTTISKE GMPMIRYRTR
     DLTVLDRSPC GCGRTLVRMS KVMGRSDDML IIRGVNVFPS QIESVLLGLG ETSPHYQLIV
     DRQGHLDTLT VMVEISEAMF SDEVRRLEML ERKIQTELAS VLKITAKVRL VAAKTLERSE
     GKAKRVIDNR QI
//
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