ID   4CL1_SOYBN              Reviewed;         293 AA.
AC   P31686;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, 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;
DE   AltName: Full=Clone 4CL14;
DE   Flags: Fragment;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Harosoy 63;
RX   PubMed=8278545; DOI=10.1104/pp.102.4.1147;
RA   Uhlmann A., Ebel J.;
RT   "Molecular cloning and expression of 4-coumarate:coenzyme A ligase, an
RT   enzyme involved in the resistance response of soybean (Glycine max L.)
RT   against pathogen attack.";
RL   Plant Physiol. 102:1147-1156(1993).
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; X69954; CAA49575.1; -; mRNA.
DR   PIR; S31705; S31705.
DR   AlphaFoldDB; P31686; -.
DR   SMR; P31686; -.
DR   STRING; 3847.GLYMA13G44950.1; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   UniPathway; UPA00372; UER00547.
DR   Proteomes; UP000008827; Unplaced.
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:0016405; F:CoA-ligase activity; IBA:GO_Central.
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; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Nucleotide-binding; Phenylpropanoid metabolism;
KW   Reference proteome.
FT   CHAIN           <1..293
FT                   /note="4-coumarate--CoA ligase 1"
FT                   /id="PRO_0000193038"
FT   NON_TER         1
SQ   SEQUENCE   293 AA;  32027 MW;  25868497FCC022EC CRC64;
     AKATILLMPK FDINSLLALI HKHKVTIAPV VPPIVLAISK SPDLHKYDLS SIRVLKSGGA
     PLGKELEDTL RAKFPNAKLG QGYGMTEAGP VLTMSLAFAK EPIDVKPGAC GTVVRNAEMK
     IVDPETGHSL PRNQSGEICI RGDQIMKGYL NDGEATERTI DKDGWLHTGD IGYIDDDDEL
     FIVDRLKELI KYKGFQVAPA ELEALLLTHP KISDAAVVPM KDEAAGEVPV AFVVISNGYT
     DTTEDEIKQF ISKQVVFYKR INRVFFIDAI PKSPSGKILR KDLRAKIAAS VPK