ID   GH36_ARATH              Reviewed;         612 AA.
AC   Q9LSQ4; Q8VYV6;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Indole-3-acetic acid-amido synthetase GH3.6;
DE            EC=6.3.2.-;
DE   AltName: Full=Auxin-responsive GH3-like protein 6;
DE            Short=AtGH3-6;
DE   AltName: Full=Protein DWARF IN LIGHT 1;
DE            Short=DFL-1;
GN   Name=GH3.6; Synonyms=DFL1; OrderedLocusNames=At5g54510; ORFNames=F24B18.13;
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], FUNCTION, AND INDUCTION.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=11169197; DOI=10.1046/j.1365-313x.2001.00957.x;
RA   Nakazawa M., Yabe N., Ichikawa T., Yamamoto Y.Y., Yoshizumi T.,
RA   Hasunuma K., Matsui M.;
RT   "DFL1, an auxin-responsive GH3 gene homologue, negatively regulates shoot
RT   cell elongation and lateral root formation, and positively regulates the
RT   light response of hypocotyl length.";
RL   Plant J. 25:213-221(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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   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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, CHARACTERIZATION, AND INDUCTION.
RX   PubMed=15659623; DOI=10.1105/tpc.104.026690;
RA   Staswick P.E., Serban B., Rowe M., Tiryaki I., Maldonado M.T.,
RA   Maldonado M.C., Suza W.;
RT   "Characterization of an Arabidopsis enzyme family that conjugates amino
RT   acids to indole-3-acetic acid.";
RL   Plant Cell 17:616-627(2005).
RN   [7]
RP   NOMENCLATURE.
RX   PubMed=12036261; DOI=10.1023/a:1015207114117;
RA   Hagen G., Guilfoyle T.J.;
RT   "Auxin-responsive gene expression: genes, promoters and regulatory
RT   factors.";
RL   Plant Mol. Biol. 49:373-385(2002).
CC   -!- FUNCTION: Catalyzes the synthesis of indole-3-acetic acid (IAA)-amino
CC       acid conjugates, providing a mechanism for the plant to cope with the
CC       presence of excess auxin. Strongly reactive with Glu, Gln, Trp, Asp,
CC       Ala, Leu, Phe, Gly, Tyr, Met, Ile and Val. Little or no product
CC       formation with His, Ser, Thr, Arg, Lys, or Cys. Also active on pyruvic
CC       and butyric acid analogs of IAA, PAA and the synthetic auxin
CC       naphthaleneacetic acid (NAA). The two chlorinated synthetic auxin
CC       herbicides 2,4-D and 3,6-dichloro-o-anisic acid (dicamba) cannot be
CC       used as substrates (PubMed:15659623). Involved in auxin signal
CC       transduction. Inhibits shoot and hypocotyl cell elongation, and lateral
CC       root cell differentiation in light (PubMed:11169197).
CC       {ECO:0000269|PubMed:11169197, ECO:0000269|PubMed:15659623}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=244 nmol/min/mg enzyme with Asp as substrate (at pH 9.0);
CC       pH dependence:
CC         Optimum pH is 9.0. No activity at or below pH 7.5.;
CC   -!- TISSUE SPECIFICITY: Expressed in cotyledons, stipules, true leaves,
CC       hypocotyls, and all parts of the roots. Not detected in flowers.
CC   -!- INDUCTION: By auxin. Not regulated by light.
CC       {ECO:0000269|PubMed:11169197, ECO:0000269|PubMed:15659623}.
CC   -!- MISCELLANEOUS: The gain-of-function mutant dfl1-D (T-DNA tagging) has a
CC       short hypocotyl under blue, red and far-red light, but not in darkness,
CC       shows an exaggerated dwarf phenotype in the adult plant caused by the
CC       inhibition of cell elongation in shoots, and inhibition of the lateral
CC       root growth without any reduction of primary root length.
CC       {ECO:0000269|PubMed:11169197}.
CC   -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AB050596; BAB17304.1; -; mRNA.
DR   EMBL; AB026634; BAA97524.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96504.1; -; Genomic_DNA.
DR   EMBL; AY069892; AAL47444.1; -; mRNA.
DR   EMBL; BT021108; AAX12878.1; -; mRNA.
DR   RefSeq; NP_200262.1; NM_124831.3.
DR   AlphaFoldDB; Q9LSQ4; -.
DR   SMR; Q9LSQ4; -.
DR   BioGRID; 20783; 1.
DR   STRING; 3702.AT5G54510.1; -.
DR   PaxDb; Q9LSQ4; -.
DR   PRIDE; Q9LSQ4; -.
DR   ProteomicsDB; 221847; -.
DR   EnsemblPlants; AT5G54510.1; AT5G54510.1; AT5G54510.
DR   GeneID; 835539; -.
DR   Gramene; AT5G54510.1; AT5G54510.1; AT5G54510.
DR   KEGG; ath:AT5G54510; -.
DR   Araport; AT5G54510; -.
DR   TAIR; locus:2147314; AT5G54510.
DR   eggNOG; ENOG502QQAN; Eukaryota.
DR   HOGENOM; CLU_016249_2_1_1; -.
DR   InParanoid; Q9LSQ4; -.
DR   OMA; ESECRKT; -.
DR   OrthoDB; 374623at2759; -.
DR   PhylomeDB; Q9LSQ4; -.
DR   BioCyc; ARA:AT5G54510-MON; -.
DR   BioCyc; MetaCyc:AT5G54510-MON; -.
DR   PRO; PR:Q9LSQ4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LSQ4; baseline and differential.
DR   Genevisible; Q9LSQ4; AT.
DR   GO; GO:0005737; C:cytoplasm; ISS:TAIR.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IBA:GO_Central.
DR   GO; GO:0010279; F:indole-3-acetic acid amido synthetase activity; IDA:TAIR.
DR   GO; GO:0010252; P:auxin homeostasis; TAS:TAIR.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR   GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR   InterPro; IPR004993; GH3.
DR   PANTHER; PTHR31901; PTHR31901; 1.
DR   Pfam; PF03321; GH3; 1.
PE   1: Evidence at protein level;
KW   Ligase; Reference proteome.
FT   CHAIN           1..612
FT                   /note="Indole-3-acetic acid-amido synthetase GH3.6"
FT                   /id="PRO_0000203575"
FT   CONFLICT        604
FT                   /note="P -> H (in Ref. 4; AAL47444)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   612 AA;  68897 MW;  CD7E498E353F7144 CRC64;
     MPEAPKIAAL EVSDESLAEK NKNKLQFIED VTTNADDVQR RVLEEILSRN ADVEYLKRHG
     LEGRTDRETF KHIMPVVTYE DIQPEINRIA NGDKSQVLCS NPISEFLTSS GTSGGERKLM
     PTIEEELDRR SLLYSLLMPV MDQFVPGLDK GKGMYFLFIK SESKTPGGLP ARPVLTSYYK
     SSHFKNRPYD PYTNYTSPNQ TILCSDSYQS MYSQMLCGLC QHKEVLRVGA VFASGFIRAI
     KFLEKHWPEL ARDIRTGTLS SEITDSSVRE AVGEILKPDP KLADFVESEC RKTSWQGIIT
     RLWPNTKYVD VIVTGTMSQY IPTLDYYSNG LPLVCTMYAS SECYFGVNLR PLCKPSEVSY
     TLIPNMAYFE FLPVHRNSGV TSSISLPKAL TEKEQQELVD LVDVKLGQEY ELVVTTYAGL
     YRYRVGDVLS VAGFKNNAPQ FSFICRKNVV LSIDSDKTDE VELQNAVKNA VTHLVPFDAS
     LSEYTSYADT SSIPGHYVLF WELCLNGNTP IPPSVFEDCC LTIEESLNSV YRQGRVSDKS
     IGPLEIKMVE SGTFDKLMDY AISLGASINQ YKTPRCVKFA PIIELLNSRV VDSYFSPKCP
     KWSPGHKQWG SN