ID   4CL_PINTA               Reviewed;         537 AA.
AC   P41636;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=4CL;
OS   Pinus taeda (Loblolly pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=L.; TISSUE=Xylem;
RA   Voo K.S.;
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Needle;
RX   PubMed=9008388; DOI=10.1104/pp.113.1.65;
RA   Zhang X.H., Chiang V.L.;
RT   "Molecular cloning of 4-coumarate:coenzyme A ligase in loblolly pine and
RT   the roles of this enzyme in the biosynthesis of lignin in compression
RT   wood.";
RL   Plant Physiol. 113:65-74(1997).
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   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; U12012; AAA92668.1; -; mRNA.
DR   EMBL; U12013; AAA92669.1; -; mRNA.
DR   EMBL; U39404; AAB42382.1; -; Genomic_DNA.
DR   EMBL; U39405; AAB42383.1; -; Genomic_DNA.
DR   PIR; T09710; T09710.
DR   PIR; T09755; T09755.
DR   AlphaFoldDB; P41636; -.
DR   SMR; P41636; -.
DR   BRENDA; 6.2.1.12; 4861.
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..537
FT                   /note="4-coumarate--CoA ligase"
FT                   /id="PRO_0000193035"
FT   VARIANT         422
FT                   /note="E -> G"
SQ   SEQUENCE   537 AA;  58591 MW;  6686EB2E84C7DC43 CRC64;
     MANGIKKVEH LYRSKLPDIE ISDHLPLHSY CFERVAEFAD RPCLIDGATD RTYCFSEVEL
     ISRKVAAGLA KLGLQQGQVV MLLLPNCIEF AFVFMGASVR GAIVTTANPF YKPGEIAKQA
     KAAGARIIVT LAAYVEKLAD LQSHDVLVIT IDDAPKEGCQ HISVLTEADE TQCPAVKIHP
     DDVVALPYSS GTTGLPKGVM LTHKGLVSSV AQQVDGENPN LYFHSDDVIL CVLPLFHIYS
     LNSVLLCALR AGAATLIMQK FNLTTCLELI QKYKVTVAPI VPPIVLDITK SPIVSQYDVS
     SVRIIMSGAA PLGKELEDAL RERFPKAIFG QGYGMTEAGP VLAMNLAFAK NPFPVKSGSC
     GTVVRNAQIK ILDTETGESL PHNQAGEICI RGPEIMKGYI NDPESTAATI DEEGWLHTGD
     VEYIDDDEEI FIVDRVKEII KYKGFQVAPA ELEALLVAHP SIADAAVVPQ KHEEAGEVPV
     AFVVKSSEIS EQEIKEFVAK QVIFYKKIHR VYFVDAIPKS PSGKILRKDL RSRLAAK