ID   Q8VNW6_DELAC            Unreviewed;       723 AA.
AC   Q8VNW6;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   03-MAY-2023, entry version 84.
DE   SubName: Full=Feruloyl-CoA synthetase {ECO:0000313|EMBL:CAC83622.1};
GN   Name=fcs {ECO:0000313|EMBL:CAC83622.1};
OS   Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=80866 {ECO:0000313|EMBL:CAC83622.1};
RN   [1] {ECO:0000313|EMBL:CAC83622.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11728709;
RA   Plaggenborg R., Steinbuchel A., Priefert H.;
RT   "The coenzyme A-dependent, non-beta-oxidation pathway and not direct
RT   deacetylation is the major route for ferulic acid degradation in Delftia
RT   acidovorans.";
RL   FEMS Microbiol. Lett. 205:9-16(2001).
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DR   EMBL; AJ300832; CAC83622.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8VNW6; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   Pfam; PF13549; ATP-grasp_5; 1.
DR   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          512..563
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   723 AA;  75933 MW;  E891273ECA41078B CRC64;
     MTTTEMAAAP RPDIGRLLRP RSIAIVGASA TPGALGASVL GNLERNGFAG DIHLINPKRS
     EIAGAACLAS VDQLPEGVDV AVLAIPQPFV LDTVAHWRRR VGAAVIFSAG FAEAGERGMA
     EQREIARIAA EAGMVVEGPN CLGCINYLQR VPLTFVEVNI DAQQADATRP AIGVVSQSGA
     MMTVLCTTLA SRALPLSHAI STGNEAASHA EDYVDFLLEQ PSTRVVAMIV EQIRQPARIL
     AAVARARSLG KSVVLLHPGK STGARSAATH TGAMAGDYAL MRTKLERAGA VFAETLEELG
     DIAEIAIRCP VLPSLVRPLQ PVQPLQRELA VLGESGAFKA VTLDWAEELG LALPAIGDDD
     SPALRAALPE FVGVSNPLDL TAQGLVEPDL YFRTLDALFG DARFSTVLVG LIQGDPVTCG
     IKMPPVLRAV RELRPAKPVI VAGLDEGAAV PAEFIAEMRA LGVPYFPSTE RALRAVQRLT
     AFSQRSFERT DAQPVALTLP AGRTVVPEYE SKAVLAQAGI PFARGRLATS AEQAVAIASE
     IGWPVALKAQ SADLSHKSDA GGVILNIADA QAMGEAWGRL HANVAAYDSA IALDGVLIEA
     MGQRGLEMII GARNDPQWGP VILAGLGGVT AEIIAMRACW TPTCPPARCC ANWTACRPPL
     LHGYRGAPAL DRQALAELIV RLGQVLRGTP AIREIDLNPV IVLPEGLVVV ALDALMLVEH
     SAG
//