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Database: UniProt
Entry: Q74CE5_GEOSL
LinkDB: Q74CE5_GEOSL
Original site: Q74CE5_GEOSL 
ID   Q74CE5_GEOSL            Unreviewed;       433 AA.
AC   Q74CE5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 104.
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-1 {ECO:0000313|EMBL:AAR35106.1};
GN   OrderedLocusNames=GSU1729 {ECO:0000313|EMBL:AAR35106.1};
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR35106.1, ECO:0000313|Proteomes:UP000000577};
RN   [1] {ECO:0000313|EMBL:AAR35106.1, ECO:0000313|Proteomes:UP000000577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA
RC   {ECO:0000313|Proteomes:UP000000577};
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA   Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA   Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA   Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA   Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR35106.1; -; Genomic_DNA.
DR   RefSeq; NP_952779.1; NC_002939.5.
DR   RefSeq; WP_010942374.1; NC_002939.5.
DR   AlphaFoldDB; Q74CE5; -.
DR   SMR; Q74CE5; -.
DR   STRING; 243231.GSU1729; -.
DR   DNASU; 2685265; -.
DR   EnsemblBacteria; AAR35106; AAR35106; GSU1729.
DR   KEGG; gsu:GSU1729; -.
DR   PATRIC; fig|243231.5.peg.1770; -.
DR   eggNOG; COG1541; Bacteria.
DR   HOGENOM; CLU_035301_1_1_7; -.
DR   InParanoid; Q74CE5; -.
DR   OrthoDB; 580775at2; -.
DR   UniPathway; UPA00930; -.
DR   Proteomes; UP000000577; 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:AAR35106.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000577}.
FT   DOMAIN          88..285
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          335..431
FT                   /note="AMP-dependent ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14535"
SQ   SEQUENCE   433 AA;  48553 MW;  7311EC7524E291D7 CRC64;
     MQIWDQQYEC MQREELEQLQ LERLQATLNR AFKNVTCYRN KFTERGIVPE DIQSLDDLKK
     LPFTTKEDLR LNYPYGMFAV PLREVVRIHS SSGTTGKPTV VGYTKHDIKV WSNLVARFMT
     AAGVTHDDVV QIAFGYGLFT GAFGLHYGAE AIGASVIPMS AGNTEKQIMI MQDYKTTALV
     CTPSYAITIA DRMEKMGVDP KSLSLKVGLF GAEPWSEAMR KEIENRLFVS ATDNYGLSEI
     IGPGVAGDCE YKCGMHISED AFIAEIIDPE TGEVLPPGSV GELVLTTLTK EAFPMIRYRT
     RDITSLDYSP CACGRTNVRM KKTMGRSDDM LIVKGVNVFP SQIEEILFAI EGCEPHYQIV
     LERHGALDVL EVHIEVTENI FFDEMKKQKA FLEMVEKRID SVLGVGATVK LVEPNSIPRH
     EGKAQRVIDN RKI
//
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