4CLL3_ARATH
ID 4CLL3_ARATH Reviewed; 552 AA.
AC Q3E6Y4; F4HST6; Q9LMV7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=4-coumarate--CoA ligase-like 3;
DE EC=6.2.1.-;
GN Name=4CLL3; OrderedLocusNames=At1g20490; ORFNames=F5M15.30;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP GENE FAMILY ORGANIZATION.
RX 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-coenzyme
RT a synthetases.";
RL Plant Physiol. 132:1065-1076(2003).
RN [5]
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-coumarate:CoA
RT ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003).
RN [6]
RP INDUCTION.
RX PubMed=16963437; DOI=10.1074/jbc.m607854200;
RA Koo A.J.K., Chung H.S., Kobayashi Y., Howe G.A.;
RT "Identification of a peroxisomal acyl-activating enzyme involved in the
RT biosynthesis of jasmonic acid in Arabidopsis.";
RL J. Biol. Chem. 281:33511-33520(2006).
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- INDUCTION: By wounding or by jasmonic acid (JA) treatment.
CC {ECO:0000269|PubMed:16963437}.
CC -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC the substrate recognition, and are sufficient to confer the substrate
CC specificity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79612.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 3 genes: At1g20480, At1g20490 and At1g20500.; Evidence={ECO:0000305};
CC Sequence=AAF79612.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AEE29978.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE29978.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BX815999; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC027665; AAF79612.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29978.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX815999; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; D86338; D86338.
DR RefSeq; NP_001322801.1; NM_001332446.1.
DR RefSeq; NP_173473.2; NM_101899.4.
DR AlphaFoldDB; Q3E6Y4; -.
DR SMR; Q3E6Y4; -.
DR BioGRID; 23876; 2.
DR IntAct; Q3E6Y4; 2.
DR STRING; 3702.AT1G20490.1; -.
DR PaxDb; Q3E6Y4; -.
DR PRIDE; Q3E6Y4; -.
DR GeneID; 838637; -.
DR KEGG; ath:AT1G20490; -.
DR Araport; AT1G20490; -.
DR eggNOG; KOG1176; Eukaryota.
DR InParanoid; Q3E6Y4; -.
DR OrthoDB; 298283at2759; -.
DR PhylomeDB; Q3E6Y4; -.
DR BioCyc; ARA:AT1G20490-MON; -.
DR PRO; PR:Q3E6Y4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q3E6Y4; baseline and differential.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
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; Peroxisome; Reference proteome.
FT CHAIN 1..552
FT /note="4-coumarate--CoA ligase-like 3"
FT /id="PRO_0000299176"
FT REGION 275..346
FT /note="SBD1"
FT /evidence="ECO:0000250"
FT REGION 347..411
FT /note="SBD2"
FT /evidence="ECO:0000250"
FT MOTIF 550..552
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 207..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 347..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 552 AA; 60499 MW; 8E4D96B2645B6254 CRC64;
MAYPERDLIV DPRSGFCKSN STFYSKRNPL CLPPNPSLDV TTFISSQPQR GTTAFIDAST
GHRLTFSDLW RVVDRVADCL YHEVGIRRGD VVLILSPNSI YIPVVCLSVM SLGAVVTTAN
TLNTSGEISK QIAQSNPTLV FTTSQLAPKL AAAISVVLTD EEDEKRVELT SGVRVVGILS
EMMKKETSGQ RVRDRVNQDD TAMMLYSSGT TGTSKGVISS HRNLTAYVAK YIDDKWKRDE
IFVCTVPMFH SFGLLAFAMG SVASGSTVVI LRRFGLDDMM QAVEKYKATI LSLAPPVLVA
MINGADQLKA KYDLTSLRKV RCGGAPLSKE VMDSFLEKYP TVNIFQGYAL TESHGSGAST
ESVEESLKYG AVGLLSSGIE ARIVDPDTGR VMGVNQPGEL WLKGPSISKG YFGNEEATNE
TINLEGWLKL GDLCYIDEDG FLFVVDRLKE LIKYKGYQVP PAELEALLIA HPHILDAAVI
PFPDREAGQY PMAYVARKPE SNLSEKEVID FISNQVAPYK KIRKVAFISS IPKTASGKTL
RKDLIKLSTS KL
