4CLL2_ARATH
ID 4CLL2_ARATH Reviewed; 565 AA.
AC Q84P25; Q9LMV7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=4-coumarate--CoA ligase-like 2;
DE EC=6.2.1.-;
GN Name=4CLL2; OrderedLocusNames=At1g20480; ORFNames=F5M15.29;
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 [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 [3]
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 [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).
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
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};
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DR EMBL; AY250833; AAP03016.1; -; mRNA.
DR EMBL; AC027665; AAF79612.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29977.1; -; Genomic_DNA.
DR PIR; D86338; D86338.
DR RefSeq; NP_173472.1; NM_101898.4.
DR AlphaFoldDB; Q84P25; -.
DR SMR; Q84P25; -.
DR BioGRID; 23875; 2.
DR IntAct; Q84P25; 2.
DR STRING; 3702.AT1G20480.1; -.
DR PaxDb; Q84P25; -.
DR PRIDE; Q84P25; -.
DR ProteomicsDB; 245163; -.
DR EnsemblPlants; AT1G20480.1; AT1G20480.1; AT1G20480.
DR GeneID; 838636; -.
DR Gramene; AT1G20480.1; AT1G20480.1; AT1G20480.
DR KEGG; ath:AT1G20480; -.
DR Araport; AT1G20480; -.
DR TAIR; locus:2034423; AT1G20480.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; Q84P25; -.
DR OMA; HRITHIQ; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q84P25; -.
DR BioCyc; ARA:AT1G20480-MON; -.
DR PRO; PR:Q84P25; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84P25; baseline and differential.
DR Genevisible; Q84P25; 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; 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..565
FT /note="4-coumarate--CoA ligase-like 2"
FT /id="PRO_0000299175"
FT REGION 288..359
FT /note="SBD1"
FT /evidence="ECO:0000250"
FT REGION 360..424
FT /note="SBD2"
FT /evidence="ECO:0000250"
FT MOTIF 563..565
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 221..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 360..365
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 460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 13
FT /note="E -> V (in Ref. 1; AAP03016)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="R -> Q (in Ref. 1; AAP03016)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> T (in Ref. 1; AAP03016)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="V -> F (in Ref. 1; AAP03016)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="M -> V (in Ref. 1; AAP03016)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 61438 MW; 0226F2C09AA3031B CRC64;
MAVKHGVDGD GSEIESRTLA VDRKSGFCES TSIFYSKREP MALPPNQFLD VTSFIASQPH
RGKTVFVDAV TGRRLSFPEL WLGVERVAGC LYALGVRKGN VVIILSPNSI LFPIVSLSVM
SLGAIITTAN PINTSDEISK QIGDSRPVLA FTTCKLVSKL AAASNFNLPV VLMDDYHVPS
QSYGDRVKLV GRLETMIETE PSESRVKQRV NQDDTAALLY SSGTTGTSKG VMLSHRNLIA
LVQAYRARFG LEQRTICTIP MCHIFGFGGF ATGLIALGWT IVVLPKFDMA KLLSAVETHR
SSYLSLVPPI VVAMVNGANE INSKYDLSSL HTVVAGGAPL SREVTEKFVE NYPKVKILQG
YGLTESTAIA ASMFNKEETK RYGASGLLAP NVEGKIVDPD TGRVLGVNQT GELWIRSPTV
MKGYFKNKEA TASTIDSEGW LKTGDLCYID GDGFVFVVDR LKELIKCNGY QVAPAELEAL
LLAHPEIADA AVIPIPDMKA GQYPMAYIVR KVGSNLSESE IMGFVAKQVS PYKKIRKVTF
LASIPKNPSG KILRRELTKL TTSKL
