ID   Q6ANS9_DESPS            Unreviewed;       444 AA.
AC   Q6ANS9;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 89.
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   OrderedLocusNames=DP1266 {ECO:0000313|EMBL:CAG35995.1};
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG35995.1, ECO:0000313|Proteomes:UP000000602};
RN   [1] {ECO:0000313|Proteomes:UP000000602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG35995.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6ANS9; -.
DR   STRING; 177439.DP1266; -.
DR   KEGG; dps:DP1266; -.
DR   eggNOG; COG1541; Bacteria.
DR   HOGENOM; CLU_035301_1_1_7; -.
DR   UniPathway; UPA00930; -.
DR   Proteomes; UP000000602; 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};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000602}.
FT   DOMAIN          90..296
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          346..442
FT                   /note="AMP-dependent ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14535"
SQ   SEQUENCE   444 AA;  49364 MW;  7C004DE6872CACDB CRC64;
     MDIVQGDMMS VKYWDEEIET LPREGLESIQ LSRLKKLVAR MYKTVVPYRE KMEAAGVTPS
     DIKSLADLAK LPFTVKDDLR DNYPFGLFAV PMDEVVRVHA SSGTTGKPTV VGYTQDDIVL
     WSNVMARALT CAGASKKDMI HNSYGYGLFT GGLGAHYGIE RLGATVIPVS GGNTKRQITV
     MKDFGATVLL ATPSYALNLA ETMDAMGVDP ATMPLRIGVF GAEPWSENMR EEVEAKLNIK
     AVDIYGLSEV MGPGVAMECL QSERGMHISE DHFLPEIIDP VTGEVLPPGS EGELVFTTLT
     KEAFPIIRYR TRDISRLYYE KCACGRTLVR MEKVLGRTDD MLIIRGVNVF PSQVEHVLMS
     VDGVEPHYQI VVDRIGNLDT MSVQVEVSED IFSDEIRKLE KLTQFIQREI KDLLGVSCKV
     QLVESKTIQR SEGKAKRVID NRKI
//