4CL2_PETCR
ID 4CL2_PETCR Reviewed; 544 AA.
AC P14913;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=4CL2; Synonyms=4CL-2;
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; X13325; CAA31697.1; -; mRNA.
DR EMBL; X05351; CAA28960.1; -; Genomic_DNA.
DR PIR; S15695; S15695.
DR AlphaFoldDB; P14913; -.
DR SMR; P14913; -.
DR PRIDE; P14913; -.
DR BioCyc; MetaCyc:MON-18289; -.
DR BRENDA; 6.2.1.12; 4694.
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_0000193034"
SQ SEQUENCE 544 AA; 59783 MW; B477965C68F8C534 CRC64;
MGDCVAPKED LIFRSKLPDI YIPKHLPLHT YCFENISKVG DKSCLINGAT GETFTYSQVE
LLSRKVASGL NKLGIQQGDT IMLLLPNSPE YFFAFLGASY RGAISTMANP FFTSAEVIKQ
LKASLAKLII TQACYVDKVK DYAAEKNIQI ICIDDAPQDC LHFSKLMEAD ESEMPEVVID
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 KDLRAKIASG
DLPK