ID   4CL1_PETCR              Reviewed;         544 AA.
AC   P14912;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=4-coumarate--CoA ligase 1;
DE            Short=4CL 1;
DE            EC=6.2.1.12;
DE   AltName: Full=4-coumaroyl-CoA synthase 1;
GN   Name=4CL1; Synonyms=4CL-1;
OS   Petroselinum crispum (Parsley) (Petroselinum hortense).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Petroselinum.
OX   NCBI_TaxID=4043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3169018; DOI=10.1111/j.1432-1033.1988.tb14328.x;
RA   Lozoya E., Hoffmann H., Douglas C., Schulz W., Scheel D., Hahlbrock K.;
RT   "Primary structures and catalytic properties of isoenzymes encoded by the
RT   two 4-coumarate:CoA ligase genes in parsley.";
RL   Eur. J. Biochem. 176:661-667(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RX   PubMed=16453765; DOI=10.1002/j.1460-2075.1987.tb02353.x;
RA   Douglas C., Hoffmann H., Schulz W., Hahlbrock K.;
RT   "Structure and elicitor or U.V.-light-stimulated expression of two 4-
RT   coumarate:CoA ligase genes in parsley.";
RL   EMBO J. 6:1189-1195(1987).
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   -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene
CC       biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step
CC       1/2.
CC   -!- INDUCTION: By fungal elicitor and UV irradiation.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; X13324; CAA31696.1; -; mRNA.
DR   EMBL; X05350; CAA28959.1; -; Genomic_DNA.
DR   PIR; S01667; S01667.
DR   AlphaFoldDB; P14912; -.
DR   SMR; P14912; -.
DR   UniPathway; UPA00372; UER00547.
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; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
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   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Nucleotide-binding; Phenylpropanoid metabolism.
FT   CHAIN           1..544
FT                   /note="4-coumarate--CoA ligase 1"
FT                   /id="PRO_0000193033"
SQ   SEQUENCE   544 AA;  59825 MW;  22BBAD78F255D0C8 CRC64;
     MGDCVAPKED LIFRSKLPDI YIPKHLPLHT YCFENISKVG DKSCLINGAT GETFTYSQVE
     LLSRKVASGL NKLGIQQGDT IMLLLPNSPE YFFAFLGASY RGAISTMANP FFTSAEVIKQ
     LKASQAKLII TQACYVDKVK DYAAEKNIQI ICIDDAPQDC LHFSKLMEAD ESEMPEVVIN
     SDDVVALPYS SGTTGLPKGV MLTHKGLVTS VAQQVDGDNP NLYMHSEDVM ICILPLFHIY
     SLNAVLCCGL RAGVTILIMQ KFDIVPFLEL IQKYKVTIGP FVPPIVLAIA KSPVVDKYDL
     SSVRTVMSGA APLGKELEDA VRAKFPNAKL GQGYGMTEAG PVLAMCLAFA KEPYEIKSGA
     CGTVVRNAEM KIVDPETNAS LPRNQRGEIC IRGDQIMKGY LNDPESTRTT IDEEGWLHTG
     DIGFIDDDDE LFIVDRLKEI IKYKGFQVAP AELEALLLTH PTISDAAVVP MIDEKAGEVP
     VAFVVRTNGF TTTEEEIKQF VSKQVVFYKR IFRVFFVDAI PKSPSGKILR KDLRARIASG
     DLPK