4CLL4_ARATH
ID 4CLL4_ARATH Reviewed; 550 AA.
AC P0C5B6; Q9LMV7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=OPC-6:CoA ligase {ECO:0000303|PubMed:18267944};
DE EC=6.2.1.- {ECO:0000305|PubMed:18267944};
DE AltName: Full=4-coumarate--CoA ligase-like 4 {ECO:0000303|PubMed:12805634};
GN Name=4CLL4 {ECO:0000303|PubMed:12805634};
GN OrderedLocusNames=At1g20500 {ECO:0000312|Araport:AT1G20500};
GN ORFNames=F5M15.18 {ECO:0000312|EMBL:AAF79612.1};
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 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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=18267944; DOI=10.1093/jxb/erm325;
RA Kienow L., Schneider K., Bartsch M., Stuible H.-P., Weng H., Miersch O.,
RA Wasternack C., Kombrink E.;
RT "Jasmonates meet fatty acids: functional analysis of a new acyl-coenzyme A
RT synthetase family from Arabidopsis thaliana.";
RL J. Exp. Bot. 59:403-419(2008).
CC -!- FUNCTION: Contributes to jasmonic acid biosynthesis by initiating the
CC beta-oxidative chain shortening of its precursors (PubMed:18267944).
CC Acyl-coenzyme A synthetase which exhibits a high activity specifically
CC toward OPC-6 ((9R,13R)-1a,1b-dinor-10,11-dihydro-12-oxo-15-phytoenoate)
CC (PubMed:18267944). Also capable of activating sinapic acid, a cinnamic
CC acid derivative (PubMed:18267944). {ECO:0000269|PubMed:18267944}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + OPC-6 = AMP + diphosphate + OPC-6-CoA;
CC Xref=Rhea:RHEA:54956, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:138430, ChEBI:CHEBI:138431,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54957;
CC Evidence={ECO:0000269|PubMed:18267944};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=169 uM for OPC-6 {ECO:0000269|PubMed:18267944};
CC KM=182 uM for sinapic acid {ECO:0000269|PubMed:18267944};
CC Note=kcat is 1.94 sec(-1) with OPC-6 as substrate. kcat is 0.12 sec(-
CC 1) with sinapic acid as substrate. {ECO:0000269|PubMed:18267944};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305|PubMed:12819348}.
CC -!- TISSUE SPECIFICITY: Expressed at very low level in leaves.
CC {ECO:0000269|PubMed:18267944}.
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|UniProtKB:Q42524}.
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};
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DR EMBL; AC027665; AAF79612.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29979.1; -; Genomic_DNA.
DR PIR; D86338; D86338.
DR RefSeq; NP_173474.5; NM_101900.5.
DR AlphaFoldDB; P0C5B6; -.
DR SMR; P0C5B6; -.
DR STRING; 3702.AT1G20500.1; -.
DR SwissLipids; SLP:000001793; -.
DR PaxDb; P0C5B6; -.
DR PRIDE; P0C5B6; -.
DR ProteomicsDB; 245164; -.
DR EnsemblPlants; AT1G20500.1; AT1G20500.1; AT1G20500.
DR GeneID; 838638; -.
DR Gramene; AT1G20500.1; AT1G20500.1; AT1G20500.
DR KEGG; ath:AT1G20500; -.
DR Araport; AT1G20500; -.
DR TAIR; locus:2034403; AT1G20500.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; P0C5B6; -.
DR OMA; HTYGLLT; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; P0C5B6; -.
DR BioCyc; ARA:AT1G20500-MON; -.
DR SABIO-RK; P0C5B6; -.
DR PRO; PR:P0C5B6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P0C5B6; baseline and differential.
DR Genevisible; P0C5B6; AT.
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; IDA:UniProtKB.
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="OPC-6:CoA ligase"
FT /id="PRO_0000299177"
FT REGION 273..344
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 345..409
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT MOTIF 548..550
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 205..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 322..324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 344..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
SQ SEQUENCE 550 AA; 60521 MW; 1ACD57613E6D1D81 CRC64;
MAYPERSLIV DPRSGFCKSN STFYSKRQPL SLPPNLSRDV TTFISSQPHR GKTAFIDAAT
GQCLTFSDLW RAVDRVADCL YHEVGIRRGD VVLILSPNSI FIPVVCLSVM SLGAVFTTAN
TLNTSGEISK QIADSNPTLV FTTRQLAPKL PVAISVVLTD DEVYQELTSA IRVVGILSEM
VKKEPSGQRV RDRVNQDDTA MMLYSSGTTG PSKGVISSHR NLTAHVARFI SDNLKRDDIF
ICTVPMFHTY GLLTFAMGTV ALGSTVVILR RFQLHDMMDA VEKHRATALA LAPPVLVAMI
NDADLIKAKY DLSSLKTVRC GGAPLSKEVT EGFLEKYPTV DILQGYALTE SNGGGAFTNS
AEESRRYGTA GTLTSDVEAR IVDPNTGRFM GINQTGELWL KGPSISKGYF KNQEATNETI
NLEGWLKTGD LCYIDEDGFL FVVDRLKELI KYKGYQVPPA ELEALLITHP DILDAAVIPF
PDKEAGQYPM AYVVRKHESN LSEKQVIDFI SKQVAPYKKI RKVSFINSIP KTASGKTLRK
DLIKLATSKL
