ID   FCS1_UNKP               Reviewed;         707 AA.
AC   A0A2P1BT06;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Trans-feruloyl-CoA synthase FCS1 {ECO:0000305};
DE            EC=6.2.1.34 {ECO:0000269|PubMed:30802241};
DE   AltName: Full=Feruloyl coenzyme A synthetase {ECO:0000303|Ref.1};
DE   AltName: Full=Trans-feruloyl-CoA synthetase {ECO:0000305};
GN   Name=FCS1 {ECO:0000303|PubMed:30802241}; Synonyms=Fcs {ECO:0000303|Ref.1};
OS   Unknown prokaryotic organism.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=2725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tomazetto G.;
RT   "Uncultured organism feruloyl coenzyme A synthetase (fcs) gene.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   ATP-BINDING SITE, AND BIOTECHNOLOGY.
RX   PubMed=30802241; DOI=10.1371/journal.pone.0212629;
RA   Sodre V., Araujo J.N., Goncalves T.A., Vilela N., Braz A.S.K., Franco T.T.,
RA   de Oliveira Neto M., Damasio A.R.L., Garcia W., Squina F.M.;
RT   "An alkaline active feruloyl-CoA synthetase from soil metagenome as a
RT   potential key enzyme for lignin valorization strategies.";
RL   PLoS ONE 14:E0212629-E0212629(2019).
CC   -!- FUNCTION: Catalyzes the formation of feruloyl-CoA, ADP and phosphate
CC       from ferulate, CoA and ATP. {ECO:0000269|PubMed:30802241}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + ADP + phosphate;
CC         Xref=Rhea:RHEA:19389, ChEBI:CHEBI:29749, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:87305,
CC         ChEBI:CHEBI:456216; EC=6.2.1.34;
CC         Evidence={ECO:0000269|PubMed:30802241};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19390;
CC         Evidence={ECO:0000269|PubMed:30802241};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.1 mM for ferulate {ECO:0000269|PubMed:30802241};
CC       pH dependence:
CC         Optimum pH is 7.8. {ECO:0000269|PubMed:30802241};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:30802241};
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:30802241}.
CC   -!- BIOTECHNOLOGY: Catalyzes the activation of ferulate via CoA-
CC       thioesterification, a first enzymatic step for conversion of the
CC       lignin-derived ferulate into high value chemicals, such as vanillin and
CC       bioplastics. {ECO:0000269|PubMed:30802241}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the acetate CoA
CC       ligase alpha subunit family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the acetate CoA
CC       ligase beta subunit family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MG214406; AVI57390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P1BT06; -.
DR   SMR; A0A2P1BT06; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0050563; F:trans-feruloyl-CoA synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.261; -; 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   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52210; SSF52210; 2.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..707
FT                   /note="Trans-feruloyl-CoA synthase FCS1"
FT                   /id="PRO_0000447891"
FT   DOMAIN          498..549
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:30802241"
FT   BINDING         524..535
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ   SEQUENCE   707 AA;  74923 MW;  121AEAE32F0A3107 CRC64;
     MGERRFSNQQ IDRLLRPKSV AVIGASDRKG ALGATLLNNL VQYEFSGDIY PVNPKRDELL
     GLKVYHEVAE LPEGIDCAVL AIPRPFVIDT VRQLAQRGCG AVVIYSAGFS EAGEEGMKDQ
     LELAAIAAEY GMVIEGPNCL GCTNYVERVP LTFVETNMQT PPKGTRAVGI ASQSGALAAV
     LATALHPRGL YVSSSVSTGN EAASGVEDYV EWLVDDEDTH VIAMYVESLR RPKAFIAAAR
     RAHAAGKPIV MLHPGKSNKA QESAATHTGA MAGDYALMKT KLAREGVIFA DTLEELADIT
     EIALRCRALP GANMAVLGES GALRGLAFDI AEDIGLDLIH LDDDNSPALR AILPDFVPVS
     NPTDITALGL SEPEIYTKVL TALLEDERIG SVVASIIQSD PITSGIKFPH IIKVLDGGTF
     AKPLVFAGVD EGATVPKEYI DGLRKVGIPW FPSTERAYRA IARLADLSKR DLADNSGDPI
     VVPGLDAVSG VVPEYKAKEL LRPLGIAFPP SQFAANAEAA AAAARAIGYP VVMKAQAAAL
     GHKSDAGGVI LNLKTDDEVR DAFARIYGNV EAYDRSIALD GVLIEKMGKM GTEMIVGAKN
     DPQWGPVVLA GFGGVTAEIL KDVKLFTPEM DAAAVQRGLL ELKQAPILKG YRGAPALDVA
     ALAELIVQIG RVMAGNPSIR EIDLNPVIIH PAGEGVAALD ALMLVER