ID   PCL_CERS4               Reviewed;         411 AA.
AC   O54075;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=4-coumarate--CoA ligase;
DE            Short=4CL;
DE            EC=6.2.1.12;
DE   AltName: Full=4-coumaroyl-CoA synthase;
GN   Name=pcl;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RX   PubMed=9630474; DOI=10.1016/s0167-4838(98)00050-8;
RA   Kort R., Phillips-Jones M.K., Van Aalten D.M.F., Haker A., Hoffer S.M.,
RA   Hellingwerf K.J., Crielaard W.;
RT   "Sequence, chromophore extraction and 3-D model of the photoactive yellow
RT   protein from Rhodobacter sphaeroides.";
RL   Biochim. Biophys. Acta 1385:1-6(1998).
CC   -!- FUNCTION: Converts p-coumaric acid into p-coumaryl CoA. This is
CC       necessary for the activation of the photoactive yellow protein (PYP)
CC       chromophore.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:19641, ChEBI:CHEBI:12876,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:85008, ChEBI:CHEBI:456215; EC=6.2.1.12;
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Although this was cloned from strain NCIB 8253 in 1998 it was
CC       not detected as part of the complete proteome when it was sequenced in
CC       2005. {ECO:0000305}.
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DR   EMBL; AJ002398; CAA05380.1; -; Genomic_DNA.
DR   AlphaFoldDB; O54075; -.
DR   SMR; O54075; -.
DR   GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR012743; 4_coum_CoA_lig.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02372; 4_coum_CoA_lig; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Phenylpropanoid metabolism.
FT   CHAIN           1..411
FT                   /note="4-coumarate--CoA ligase"
FT                   /id="PRO_0000193045"
SQ   SEQUENCE   411 AA;  45008 MW;  0296253554395F37 CRC64;
     MTAEGPLAPE DRVLDREAIG RLCVSLIAAE QQDLLREGRV GHHQMIGARL LTAGHPSPDD
     LLIDEDTLGL DSLLMLSLVT RVAGFFHLSD SNTEDYLLVR RRLGEWVDLI DHHHTLMGPK
     ARFTFATSGS TAGPKPVTHS AAALLSEGQA IAKILTERPP EVRRVLSCVP AHHIYGFLWS
     CLFPSRRGLE AKQLANLSAS GIMRHARSGD LVVGTPFIWE QFADLDYRLP GDVVGVTSGA
     PSTAETWRCA SALGPARMLD IYGSTETGGI GWRERRDDPF RTLPDLACFH DTLSRLGRRL
     DLQDEIAWDK DGGFTILGRK DEILQVAGSN VSPAAVRDIL LRNPRVRDAA VRLDGRRLKA
     VISVAEGADE AEIEIELRAT AARHLPAPAR PDRFLFATEL PRTGAGKLAD W