ID   4CL2_SOLTU              Reviewed;         545 AA.
AC   P31685;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=4-coumarate--CoA ligase 2;
DE            Short=4CL 2;
DE            EC=6.2.1.12;
DE   AltName: Full=4-coumaroyl-CoA synthase 2;
GN   Name=4CL2; Synonyms=4CL-2;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2022667; DOI=10.1016/s0021-9258(18)93010-3;
RA   Becker-Andre M., Schulze-Lefert P., Hahlbrock K.;
RT   "Structural comparison, modes of expression, and putative cis-acting
RT   elements of the two 4-coumarate: CoA ligase genes in potato.";
RL   J. Biol. Chem. 266:8551-8559(1991).
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   PIR; B39827; B39827.
DR   AlphaFoldDB; P31685; -.
DR   SMR; P31685; -.
DR   STRING; 4113.PGSC0003DMT400036886; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   InParanoid; P31685; -.
DR   UniPathway; UPA00372; UER00547.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P31685; baseline.
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; 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   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Phenylpropanoid metabolism;
KW   Reference proteome.
FT   CHAIN           1..545
FT                   /note="4-coumarate--CoA ligase 2"
FT                   /id="PRO_0000193037"
SQ   SEQUENCE   545 AA;  59625 MW;  5481F0B0AFEA39E0 CRC64;
     MPMDIETKQS GDLIFRSKLP DIYIPKHLPL HSYCFENLSE FNSRPCLIDG ANDRIYTYAE
     VELTSRKVAV GLNKLGIQQK DTIMILLPNC PEFVFAFIGA SYLGAISTMA NPLFTPAEVV
     KQAKASSAKI VITQACFAGK VKDYAIENDL KVICVDSAPE GCVHFSELIQ SDEHEIPDVK
     IQPDDVVALP YSSGTTGLPK GVMLTHKGLV TSVAQQVDGE NANLYMHSDD VLMCVLPLFH
     IYSLNSVLLC ALRVGAAILI MQKFDIAQFL ELIPKHKVTI GPFVPPIVLA IAKSPLVHNY
     DLSSVRTVMS GAAPLGKELE DAVRAKFPNA KLGQGYGMTE AGPVLAMCLA FAKEPFDIKS
     GACGTVVRNA EMKIVDPDTG CSLPRNQPGE ICIRGDQIMK GYLNDPEATA RTIEKEGWLH
     TGDIGFIDDD DELFIVDRLK ELIKYKGFQV APAELEALLI NHPDISDAAV VPMIDEQAGE
     VPVAFVVRSN GSTITEDEVK DFISKQVIFY KRIKRVFFVE TVPKSPSGKI LRKDLRARLA
     AGISN