GH39_ARATH
ID GH39_ARATH Reviewed; 585 AA.
AC O82243;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Putative indole-3-acetic acid-amido synthetase GH3.9;
DE EC=6.3.2.-;
DE AltName: Full=Auxin-responsive GH3-like protein 9;
DE Short=AtGH3-9;
GN Name=GH3.9; OrderedLocusNames=At2g47750; ORFNames=F17A22.14;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [4]
RP IDENTIFICATION, 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 [5]
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. {ECO:0000250}.
CC -!- INDUCTION: Not induced by auxin. {ECO:0000269|PubMed:15659623}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {ECO:0000305}.
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DR EMBL; AC005309; AAC63630.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10882.1; -; Genomic_DNA.
DR EMBL; AY054288; AAL06947.1; -; mRNA.
DR EMBL; BT000629; AAN18195.1; -; mRNA.
DR PIR; A84919; A84919.
DR RefSeq; NP_182296.1; NM_130342.3.
DR AlphaFoldDB; O82243; -.
DR SMR; O82243; -.
DR BioGRID; 4722; 2.
DR IntAct; O82243; 1.
DR STRING; 3702.AT2G47750.1; -.
DR PaxDb; O82243; -.
DR PRIDE; O82243; -.
DR ProteomicsDB; 220752; -.
DR EnsemblPlants; AT2G47750.1; AT2G47750.1; AT2G47750.
DR GeneID; 819387; -.
DR Gramene; AT2G47750.1; AT2G47750.1; AT2G47750.
DR KEGG; ath:AT2G47750; -.
DR Araport; AT2G47750; -.
DR TAIR; locus:2043308; AT2G47750.
DR eggNOG; ENOG502QPMW; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; O82243; -.
DR OMA; KPLCDPA; -.
DR OrthoDB; 374623at2759; -.
DR PhylomeDB; O82243; -.
DR PRO; PR:O82243; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82243; baseline and differential.
DR Genevisible; O82243; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IBA:GO_Central.
DR InterPro; IPR004993; GH3.
DR PANTHER; PTHR31901; PTHR31901; 1.
DR Pfam; PF03321; GH3; 1.
PE 2: Evidence at transcript level;
KW Ligase; Reference proteome.
FT CHAIN 1..585
FT /note="Putative indole-3-acetic acid-amido synthetase
FT GH3.9"
FT /id="PRO_0000203576"
SQ SEQUENCE 585 AA; 66158 MW; 862F41C8401E148F CRC64;
MDVMKLDHDS VLKELERITS KAAEVQDNIL RGILERNKDT EYLSKYMNGS KDVLEFKRAV
PIIIYKDIYP YIQRIANGED SSLITGHSIT EILCSSGTSA GEPKLMPTIP EDLDRRTFLY
NLIIPIVNKY ITGLDKGKAM YLNFVKAETS TPCGLPIRAV LTSYYKSKHF QCRPYDPFND
LTSPIQTILC EDSNQSMYCQ LLAGLIHRHK VMRLGAVFAS AFLRAISYLE KKWSQLCEDI
RTGSLNPMIT DPGCQMAMSC LLMSPNPELA SEIEEICGRS SWKGILCQLW PKAKFIEAVV
TGSMAQYIPA LEFFSQGKIP LVCPMYASSE TYFGVNVEPL SKPSDVVFTL LPNMCYFEFI
PLGKNGTLSF DLDDDEQVPC DKVVDLVNVK LGRYYELVVT TFAGLYRYRI GDVLQVAGFY
NGAPQFRFIC RRNVVLSIDL DKTNEEDLHR SITLAKKKLG SNAFLAEYTS YADTSSVPGH
YVLFWEIQGH LEPKLMEECC VAVEEELDYI YRQCRTKERS IGALEIRVVK PGTFEKLMDL
IISQGGSFNQ YKTPRCVKSN SATFKLLNGH VMASFFSPRD PTWVP
