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 01-MAY-2013, entry version 66.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
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-
RT coenzyme 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
RT ligase 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
RT P1 clones.";
RL DNA Res. 4:215-230(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.,
RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA Shibata K., 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.,
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 [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-
RT coumarate:CoA 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
RT the biosynthesis of jasmonic acid in Arabidopsis.";
RL J. Biol. Chem. 281:33511-33520(2006).
CC -!- SUBCELLULAR LOCATION: Peroxisome (Potential).
CC -!- INDUCTION: By wounding or by jasmonic acid (JA) treatment.
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 (By similarity).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11279.1; Type=Erroneous gene model prediction;
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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 IPI; IPI00541377; -.
DR RefSeq; NP_198628.2; NM_123172.3.
DR UniGene; At.30435; -.
DR UniGene; At.68167; -.
DR HSSP; P08659; 1LCI.
DR ProteinModelPortal; Q84P26; -.
DR SMR; Q84P26; 24-542.
DR EnsemblPlants; AT5G38120.1; AT5G38120.1; AT5G38120.
DR GeneID; 833792; -.
DR KEGG; ath:AT5G38120; -.
DR TAIR; At5g38120; -.
DR eggNOG; COG0318; -.
DR HOGENOM; HOG000230009; -.
DR InParanoid; Q84P26; -.
DR OMA; VAHCRAN; -.
DR PhylomeDB; Q84P26; -.
DR ProtClustDB; CLSN2679410; -.
DR Genevestigator; Q84P26; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR025110; DUF4009.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; DUF4009; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW Peroxisome; Reference proteome.
FT CHAIN 1 550 4-coumarate--CoA ligase-like 8.
FT /FTId=PRO_0000299181.
FT NP_BIND 207 215 ATP (By similarity).
FT NP_BIND 348 353 ATP (By similarity).
FT REGION 276 347 SBD1 (By similarity).
FT REGION 348 412 SBD2 (By similarity).
FT MOTIF 548 550 Microbody targeting signal (Potential).
FT BINDING 430 430 ATP (By similarity).
FT BINDING 445 445 ATP (By similarity).
FT BINDING 536 536 ATP (By similarity).
FT CONFLICT 72 72 M -> R (in Ref. 1; AAP03015).
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
//
