ID   4CL1_ARATH              Reviewed;         561 AA.
AC   Q42524; Q8RY63;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 73.
DE   RecName: Full=4-coumarate--CoA ligase 1;
DE            Short=4CL 1;
DE            EC=6.2.1.12;
DE   AltName: Full=4-coumarate--CoA ligase isoform 1;
DE            Short=At4CL1;
DE   AltName: Full=4-coumaroyl-CoA synthase 1;
GN   Name=4CL1; OrderedLocusNames=At1g51680; ORFNames=F19C24.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=95367648; PubMed=7640359; DOI=10.1007/BF00042072;
RA   Lee D., Ellard M., Wanner L.A., Davis K.R., Douglas C.J.;
RT   "The Arabidopsis thaliana 4-coumarate:CoA ligase (4CL) gene: stress
RT   and developmentally regulated expression and nucleotide sequence of
RT   its cDNA.";
RL   Plant Mol. Biol. 28:871-884(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION, AND
RP   ENZYME ACTIVITY.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=99348176; PubMed=10417722;
RX   DOI=10.1046/j.1365-313X.1999.00491.x;
RA   Ehlting J., Buettner D., Wang Q., Douglas C.J., Somssich I.E.,
RA   Kombrink E.;
RT   "Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana
RT   represent two evolutionarily divergent classes in angiosperms.";
RL   Plant J. 19:9-20(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Lawrence P.K.;
RT   "Functional classification of Arabidopsis thaliana 4-coumarate CoA
RT   ligase genes.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   SUBSTRATE-BINDING DOMAINS.
RX   PubMed=11576429; DOI=10.1046/j.1365-313X.2001.01122.x;
RA   Ehlting J., Shin J.J.K., Douglas C.J.;
RT   "Identification of 4-coumarate:coenzyme A ligase (4CL) substrate
RT   recognition domains.";
RL   Plant J. 27:455-465(2001).
RN   [7]
RP   GENE FAMILY ORGANIZATION.
RX   MEDLINE=22690213; PubMed=12805634; DOI=10.1104/pp.103.020552;
RA   Shockey J.M., Fulda M.S., Browse J.;
RT   "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT   Phylogenetic and biochemical analysis reveals a new class of acyl-
RT   coenzyme a synthetases.";
RL   Plant Physiol. 132:1065-1076(2003).
RN   [8]
RP   GENE FAMILY ORGANIZATION.
RX   PubMed=12819348; DOI=10.1073/pnas.1430550100;
RA   Schneider K., Hoevel K., Witzel K., Hamberger B., Schomburg D.,
RA   Kombrink E., Stuible H.-P.;
RT   "The substrate specificity-determining amino acid code of 4-
RT   coumarate:CoA ligase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=15677481; DOI=10.1074/jbc.M413578200;
RA   Schneider K., Kienow L., Schmelzer E., Colby T., Bartsch M.,
RA   Miersch O., Wasternack C., Kombrink E., Stuible H.-P.;
RT   "A new type of peroxisomal acyl-coenzyme A synthetase from Arabidopsis
RT   thaliana has the catalytic capacity to activate biosynthetic
RT   precursors of jasmonic acid.";
RL   J. Biol. Chem. 280:13962-13972(2005).
RN   [10]
RP   INDUCTION BY WOUNDING.
RX   PubMed=16738863; DOI=10.1007/s00425-006-0296-y;
RA   Soltani B.M., Ehlting J., Hamberger B., Douglas C.J.;
RT   "Multiple cis-regulatory elements regulate distinct and complex
RT   patterns of developmental and wound-induced expression of Arabidopsis
RT   thaliana 4CL gene family members.";
RL   Planta 224:1226-1238(2006).
CC   -!- FUNCTION: Produces CoA thioesters of a variety of hydroxy- and
CC       methoxy-substituted cinnamic acids, which are used to synthesize
CC       several phenylpropanoid-derived compounds, including anthocyanins,
CC       flavonoids, isoflavonoids, coumarins, lignin, suberin and wall-
CC       bound phenolics.
CC   -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate +
CC       4-coumaroyl-CoA.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6320 uM for cinnamate;
CC         KM=38 uM for 4-coumarate;
CC         KM=11 uM for caffeate;
CC         KM=199 uM for ferulate;
CC   -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene
CC       biosynthesis; 3,4',5-trihydroxystilbene from 4-coumaric acid: step
CC       1/2.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q42524-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q42524-2; Sequence=VSP_008911;
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in roots, bolting
CC       stems and siliques. Also detected in leaves.
CC   -!- INDUCTION: By wounding, UV irradiation, and pathogen attack.
CC   -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are
CC       involved in the substrate recognition, and are sufficient to
CC       confer the substrate specificity.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
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DR   EMBL; U18675; AAA82888.1; -; mRNA.
DR   EMBL; AF106084; AAD47191.1; -; Genomic_DNA.
DR   EMBL; AY376729; AAQ86588.1; -; mRNA.
DR   EMBL; AC025294; AAG50881.1; -; Genomic_DNA.
DR   EMBL; AY075622; AAL91633.1; -; mRNA.
DR   EMBL; AY099747; AAM20598.1; -; mRNA.
DR   EMBL; AY133582; AAM91412.1; -; mRNA.
DR   IPI; IPI00532346; -.
DR   IPI; IPI00547355; -.
DR   PIR; S57784; S57784.
DR   RefSeq; NP_175579.1; -.
DR   UniGene; At.21694; -.
DR   HSSP; P08659; 1LCI.
DR   TCDB; 4.C.1.1.7; proposed fatty acid transporter (FAT) family.
DR   PRIDE; Q42524; -.
DR   GeneID; 841593; -.
DR   GenomeReviews; CT485782_GR; AT1G51680.
DR   NMPDR; fig|3702.1.peg.4642; -.
DR   TAIR; At1g51680; -.
DR   OMA; Q42524; ISAMLDI.
DR   BioCyc; MetaCyc:AT1G51680-MON; -.
DR   BRENDA; 6.2.1.12; 302.
DR   ArrayExpress; Q42524; -.
DR   GermOnline; AT1G51680; Arabidopsis thaliana.
DR   GO; GO:0016207; F:4-coumarate-CoA ligase activity; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Complete proteome; Ligase;
KW   Nucleotide-binding; Phenylpropanoid metabolism.
FT   CHAIN         1    561       4-coumarate--CoA ligase 1.
FT                                /FTId=PRO_0000193027.
FT   NP_BIND     210    218       ATP (By similarity).
FT   NP_BIND     353    358       ATP (By similarity).
FT   REGION      283    352       SBD1.
FT   REGION      353    420       SBD2.
FT   BINDING     441    441       ATP (By similarity).
FT   BINDING     456    456       ATP (By similarity).
FT   BINDING     547    547       ATP (By similarity).
FT   VAR_SEQ     491    561       Missing (in isoform 2).
FT                                /FTId=VSP_008911.
SQ   SEQUENCE   561 AA;  61053 MW;  5A9E20816D0C0D07 CRC64;
     MAPQEQAVSQ VMEKQSNNNN SDVIFRSKLP DIYIPNHLSL HDYIFQNISE FATKPCLING
     PTGHVYTYSD VHVISRQIAA NFHKLGVNQN DVVMLLLPNC PEFVLSFLAA SFRGATATAA
     NPFFTPAEIA KQAKASNTKL IITEARYVDK IKPLQNDDGV VIVCIDDNES VPIPEGCLRF
     TELTQSTTEA SEVIDSVEIS PDDVVALPYS SGTTGLPKGV MLTHKGLVTS VAQQVDGENP
     NLYFHSDDVI LCVLPMFHIY ALNSIMLCGL RVGAAILIMP KFEINLLLEL IQRCKVTVAP
     MVPPIVLAIA KSSETEKYDL SSIRVVKSGA APLGKELEDA VNAKFPNAKL GQGYGMTEAG
     PVLAMSLGFA KEPFPVKSGA CGTVVRNAEM KIVDPDTGDS LSRNQPGEIC IRGHQIMKGY
     LNNPAATAET IDKDGWLHTG DIGLIDDDDE LFIVDRLKEL IKYKGFQVAP AELEALLIGH
     PDITDVAVVA MKEEAAGEVP VAFVVKSKDS ELSEDDVKQF VSKQVVFYKR INKVFFTESI
     PKAPSGKILR KDLRAKLANG L
//