ID   4CL1_TOBAC              Reviewed;         547 AA.
AC   O24145;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 77.
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;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8819324; DOI=10.1104/pp.112.1.193;
RA   Lee D., Douglas C.J.;
RT   "Two divergent members of a tobacco 4-coumarate:coenzyme A ligase (4CL)
RT   gene family. cDNA structure, gene inheritance and expression, and
RT   properties of recombinant proteins.";
RL   Plant Physiol. 112:193-205(1996).
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; U50845; AAB18637.1; -; mRNA.
DR   RefSeq; NP_001312667.1; NM_001325738.1.
DR   AlphaFoldDB; O24145; -.
DR   SMR; O24145; -.
DR   STRING; 4097.O24145; -.
DR   GeneID; 107803673; -.
DR   KEGG; nta:107803673; -.
DR   OMA; HLAKMVP; -.
DR   PhylomeDB; O24145; -.
DR   UniPathway; UPA00372; UER00547.
DR   Proteomes; UP000084051; 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; 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;
KW   Reference proteome.
FT   CHAIN           1..547
FT                   /note="4-coumarate--CoA ligase 1"
FT                   /id="PRO_0000193040"
SQ   SEQUENCE   547 AA;  59842 MW;  154DF6D684E3F51B CRC64;
     MPMETTTETK QSGDLIFRSK LPDIYIPKHL PLHSYCFENI SEFSSRPCLI NGANDQIYTY
     AEVELTCRKV AVGLNKLGIQ QKDTIMILLP NSPEFVFAFM GASYLGAIST MANPLFTPAE
     VVKQAKASSA KIIITQSCFV GKVKDYASEN DVKVICIDSA PEGCLHFSEL TQSDEHEIPE
     VKIQPDDVVA LPYSSGTTGL PKGVMLTHKG LVTSVAQQVD GENANLYMHS EDVLMCVLPL
     FHIYSLNSIL LCGLRVGAAI LIMQKFDIAP FLELIQKYKV SIGPFVPPIV LAIAKSPIVD
     SYDLSSVRTV MSGAAPLGKE LEDAVRTKFP NAKLGQGYGM TEAGPVLAMC LAFAKEPFDI
     KSGACGTVVR NAEMKIVDPD TGCSLPRNQP GEICIRGDQI MKGYLNDPEA TTRTIDKEGW
     LHTGDIGFID EDDELFIVDR LKELIKYKGF QVAPAEIEAL LLNHPNISDA AVVPMKDEQA
     GEVPVAFVVR SNGSAITEDE VKDFISKQVI FYKRVKRVFF VETVPKSPSG KILRKDLRAR
     LAAGVPN