4CLL8_ARATH
ID 4CLL8_ARATH Reviewed; 550 AA.
AC Q84P26; Q8GXU2; Q9FF44;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=4-coumarate--CoA ligase-like 8;
DE EC=6.2.1.-;
DE AltName: Full=4-coumarate--CoA ligase isoform 11;
DE Short=At4CL11;
GN Name=4CLL8; OrderedLocusNames=At5g38120; ORFNames=MXA21.23, MXA21_10;
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 [MRNA], AND GENE FAMILY ORGANIZATION.
RC STRAIN=cv. Wassilewskija;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lawrence P.K.;
RT "Functional classification of Arabidopsis thaliana 4-coumarate CoA ligase
RT genes.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
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 [8]
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=BAB11279.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY250832; AAP03015.1; -; mRNA.
DR EMBL; AY376735; AAQ86594.1; -; mRNA.
DR EMBL; AB005247; BAB11279.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94270.1; -; Genomic_DNA.
DR EMBL; AK118041; BAC42672.1; -; mRNA.
DR EMBL; BT005689; AAO64109.1; -; mRNA.
DR RefSeq; NP_198628.2; NM_123172.4.
DR AlphaFoldDB; Q84P26; -.
DR SMR; Q84P26; -.
DR STRING; 3702.AT5G38120.1; -.
DR PaxDb; Q84P26; -.
DR PRIDE; Q84P26; -.
DR ProteomicsDB; 245138; -.
DR EnsemblPlants; AT5G38120.1; AT5G38120.1; AT5G38120.
DR GeneID; 833792; -.
DR Gramene; AT5G38120.1; AT5G38120.1; AT5G38120.
DR KEGG; ath:AT5G38120; -.
DR Araport; AT5G38120; -.
DR TAIR; locus:2176662; AT5G38120.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; Q84P26; -.
DR OMA; SEMMNKE; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q84P26; -.
DR BioCyc; ARA:AT5G38120-MON; -.
DR PRO; PR:Q84P26; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84P26; baseline and differential.
DR Genevisible; Q84P26; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IMP:TAIR.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:TAIR.
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..550
FT /note="4-coumarate--CoA ligase-like 8"
FT /id="PRO_0000299181"
FT REGION 276..347
FT /note="SBD1"
FT /evidence="ECO:0000250"
FT REGION 348..412
FT /note="SBD2"
FT /evidence="ECO:0000250"
FT MOTIF 548..550
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 348..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 72
FT /note="M -> R (in Ref. 1; AAP03015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 60393 MW; F1E2D4A82864C623 CRC64;
MANSQRSSSL IDPRNGFCTS NSTFYSKRKP LALPSKESLD ITTFISSQTY RGKTAFIDAA
TDHRISFSDL WMAVDRVADC LLHDVGIRRG DVVLVLSPNT ISIPIVCLSV MSLGAVLTTA
NPLNTASEIL RQIADSNPKL AFTTPELAPK IASSGISIVL ERVEDTLRVP RGLKVVGNLT
EMMKKEPSGQ AVRNQVHKDD TAMLLYSSGT TGRSKGVNSS HGNLIAHVAR YIAEPFEQPQ
QTFICTVPLF HTFGLLNFVL ATLALGTTVV ILPRFDLGEM MAAVEKYRAT TLILVPPVLV
TMINKADQIM KKYDVSFLRT VRCGGAPLSK EVTQGFMKKY PTVDVYQGYA LTESNGAGAS
IESVEESRRY GAVGLLSCGV EARIVDPNTG QVMGLNQTGE LWLKGPSIAK GYFRNEEEII
TSEGWLKTGD LCYIDNDGFL FIVDRLKELI KYKGYQVPPA ELEALLLNHP DILDAAVIPF
PDKEAGQFPM AYVARKPESN LCEKKVIDFI SKQVAPYKKI RKVAFIDSIP KTPSGKTLRK
DLIKFAISKI
