SWISSPROT: D3UY90_XENBS

ID   D3UY90_XENBS            Unreviewed;       435 AA.
AC   D3UY90;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 44.
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:CBJ79268.1};
GN   OrderedLocusNames=XBJ1_0117 {ECO:0000313|EMBL:CBJ79268.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79268.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79268.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79268.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667741; CBJ79268.1; -; Genomic_DNA.
DR   RefSeq; WP_012986735.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0117; -.
DR   EnsemblBacteria; CBJ79268; CBJ79268; XBJ1_0117.
DR   GeneID; 8829741; -.
DR   KEGG; xbo:XBJ1_0117; -.
DR   PATRIC; fig|406818.4.peg.104; -.
DR   eggNOG; ENOG4105DZS; Bacteria.
DR   eggNOG; COG1541; LUCA.
DR   HOGENOM; HOG000197614; -.
DR   KO; K01912; -.
DR   OMA; GSHIWED; -.
DR   BioCyc; XBOV406818:XBJ1_RS00515-MONOMER; -.
DR   UniPathway; UPA00930; -.
DR   Proteomes; UP000002045; 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   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR028154; AMP-dep_Lig_C.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; AMP-dep_Synthh-like_sf.
DR   InterPro; IPR011880; PA_CoA_ligase.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF14535; AMP-binding_C_2; 1.
DR   PIRSF; PIRSF006444; PaaK; 1.
DR   TIGRFAMs; TIGR02155; PA_CoA_ligase; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UY90.
DR   SWISS-2DPAGE; D3UY90.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Ligase {ECO:0000256|PIRNR:PIRNR006444, ECO:0000313|EMBL:CBJ79268.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN       81    290       AMP-binding. {ECO:0000259|Pfam:PF00501}.
FT   DOMAIN      337    432       AMP-binding_C_2. {ECO:0000259|Pfam:
FT                                PF14535}.
SQ   SEQUENCE   435 AA;  49216 MW;  13C61A342DA73073 CRC64;
     MSNNVQHLDS IEFASRDEIQ AHQFEQIKWT LHHAYNNVPM YRRKFDTAGI HPSDFRQLAD
     ITKFPYTTKQ DLRDHYPFDT FAVPMEQIVR IHASSGTTGH PTVVGYTQRD IDHWANLVAR
     CLRFAGASAK DKVHVAYGYG LFTGGLGAHY GAERLGATVI PMSGGQTEKQ AQLILDFKPD
     VIMMTPSYCL TLLDALEQRM GGDASKCSLR VGIFGAEPWT EALRSEIETR MGIKALDIYG
     LSEVMGPGIA MESVEHANGS TIWEDHFYPE VIEPDNLNVL PDGESGELVF TTLTKEAMPV
     IRYRTRDLTR LLPGTARHMR RMDRIAGRSD DMLIIRGINV FPSQVEEQII RFKELSPHYQ
     LEVNRTGNYD CLSVKVELKE PERLDAQQRC DICHQLRHHI KSMIGLSTEV SIVNCGDIPR
     SEGKAVRVID HRQHE
//