4CLL1_ARATH
ID 4CLL1_ARATH Reviewed; 542 AA.
AC Q9LQ12;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=4-coumarate--CoA ligase-like 1;
DE EC=6.2.1.-;
DE AltName: Full=4-coumarate--CoA ligase isoform 10;
DE Short=At4CL10;
GN Name=4CLL1; Synonyms=ACOS5 {ECO:0000303|PubMed:23632852};
GN OrderedLocusNames=At1g62940; ORFNames=F16P17.9;
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 (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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 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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH TKPR1; PKSA
RP AND PKSB.
RX PubMed=23632852; DOI=10.1104/pp.112.213124;
RA Lallemand B., Erhardt M., Heitz T., Legrand M.;
RT "Sporopollenin biosynthetic enzymes interact and constitute a metabolon
RT localized to the endoplasmic reticulum of tapetum cells.";
RL Plant Physiol. 162:616-625(2013).
CC -!- SUBUNIT: Interacts with TKPR1, PKSA and PKSB.
CC {ECO:0000269|PubMed:23632852}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:23632852}.
CC -!- TISSUE SPECIFICITY: Mostly confined to anther tapetal cells.
CC {ECO:0000269|PubMed:23632852}.
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}.
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DR EMBL; AY250836; AAP03019.1; -; mRNA.
DR EMBL; AY376734; AAQ86593.1; -; mRNA.
DR EMBL; AC011000; AAF75805.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34025.1; -; Genomic_DNA.
DR PIR; B96654; B96654.
DR RefSeq; NP_176482.1; NM_104972.3.
DR AlphaFoldDB; Q9LQ12; -.
DR SMR; Q9LQ12; -.
DR STRING; 3702.AT1G62940.1; -.
DR PaxDb; Q9LQ12; -.
DR PRIDE; Q9LQ12; -.
DR ProteomicsDB; 245089; -.
DR EnsemblPlants; AT1G62940.1; AT1G62940.1; AT1G62940.
DR GeneID; 842596; -.
DR Gramene; AT1G62940.1; AT1G62940.1; AT1G62940.
DR KEGG; ath:AT1G62940; -.
DR Araport; AT1G62940; -.
DR TAIR; locus:2015499; AT1G62940.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; Q9LQ12; -.
DR OMA; YIMPKFD; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q9LQ12; -.
DR BioCyc; ARA:AT1G62940-MON; -.
DR BioCyc; MetaCyc:AT1G62940-MON; -.
DR PRO; PR:Q9LQ12; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQ12; baseline and differential.
DR Genevisible; Q9LQ12; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:TAIR.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IDA:TAIR.
DR GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; IDA:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0080110; P:sporopollenin 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; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..542
FT /note="4-coumarate--CoA ligase-like 1"
FT /id="PRO_0000299174"
FT REGION 260..331
FT /note="SBD1"
FT /evidence="ECO:0000250"
FT REGION 332..399
FT /note="SBD2"
FT /evidence="ECO:0000250"
FT BINDING 189..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 332..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 542 AA; 59169 MW; 8F055B6A1E0DF85B CRC64;
MESQKQEDNE YIFRSLYPSV PIPDKLTLPE FVLQGVEEYT ENVAFVEAVT GKAVTYGDVV
RDTKRLAKAL TSLGLRKGQV MVVVLPNVAE YGIIALGIMS AGGVFSGANP TALVSEIKKQ
VEASGARGII TDATNYEKVK SLGLPVIVLG EEKIEGAVNW KDLLEAGDKC GDTDNEEILQ
TDLCALPFSS GTTGLQKGVM LTHRNLIANL CSTLFGVRSE MIGQIVTLGL IPFFHIYGIV
GICCATMKNK GKVVAMSRYD LRIFLNALIA HEVSFAPIVP PIILNLVKNP IVDEFDLSKL
KLQSVMTAAA PLAPELLTAF EAKFPNVQVQ EAYGLTEHSC ITLTHGDPEK GQGIAKRNSV
GFILPNLEVK FIDPDTGRSL PKNTSGELCV RSQCVMQGYF MNKEETDKTI DEQGWLHTGD
IGYIDDDGDI FIVDRIKELI KYKGFQVAPA ELEAILLTHP SVEDVAVVPL PDEEAGEIPA
ACVVINPKAT EKEEDILNFV AANVAHYKKV RAVHFVDSIP KSLSGKIMRR LLRDKILSIN
KK
