ID   PCL_HALHA               Reviewed;         391 AA.
AC   P42516;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=4-coumarate--CoA ligase;
DE            Short=4CL;
DE            EC=6.2.1.12;
DE   AltName: Full=4-coumaroyl-CoA synthase;
DE   Flags: Fragment;
GN   Name=pcl;
OS   Halorhodospira halophila (Ectothiorhodospira halophila).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=1053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BN9626;
RX   PubMed=8670821; DOI=10.1002/j.1460-2075.1996.tb00685.x;
RA   Kort R., Hoff W.D., van West M., Kroon A.R., Hoffer S.M., Vlieg K.H.,
RA   Crielaard W., van Beeumen J.J., Hellingwerf K.J.;
RT   "The xanthopsins: a new family of eubacterial blue-light photoreceptors.";
RL   EMBO J. 15:3209-3218(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
RC   STRAIN=BN9626;
RX   PubMed=7981196; DOI=10.1021/bi00252a001;
RA   Baca M., Borgstahl G.E., Boissinot M., Burke P.M., Williams D.R.,
RA   Slater K.A., Getzoff E.D.;
RT   "Complete chemical structure of photoactive yellow protein: novel
RT   thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry.";
RL   Biochemistry 33:14369-14377(1994).
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}.
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DR   EMBL; X98887; CAA67392.1; -; Genomic_DNA.
DR   EMBL; U17017; AAA61736.1; -; Genomic_DNA.
DR   PIR; C55993; C55993.
DR   AlphaFoldDB; P42516; -.
DR   SMR; P42516; -.
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..>391
FT                   /note="4-coumarate--CoA ligase"
FT                   /id="PRO_0000193043"
FT   NON_TER         391
SQ   SEQUENCE   391 AA;  42439 MW;  698321FB6EB2A07D CRC64;
     MQGLNADEVL RLLRSLIPGE LATGRGQRGD PPEAQDLCAD SRLDAEPIRA DSLDRLNLAS
     ALNRFFRLHE TGVEDRLLAV RRIGDMAELI ADASQHTSGL TFSTSGSTGT PQPHHHSWAA
     LTQEAEALAN ALGSHPRVIA WLPVHHLYGF VFGVALPRAL GSTVIESHAA PTALFREPAP
     DDLIATVPAR WRYLFDSNHR FPGGTGISST AALETACRNG LLQAGLDALL EVYGATEAGG
     IGLRWAPSED YRLLPHWHGD ATATSSALNP DGAAVTVAPL DRLQWRDERV FRPTGRIDDI
     IQIGGVNVSP GHVARRLESH EAVAACAVRS HGEGSRRRLK AFIVPARSDA DPETLRQTLE
     NWIWEHLPAV ERPTDLRIGT ELPRNAMGKL Q