GH33_ARATH
ID GH33_ARATH Reviewed; 595 AA.
AC O22190;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Indole-3-acetic acid-amido synthetase GH3.3;
DE EC=6.3.2.-;
DE AltName: Full=Auxin-responsive GH3-like protein 3;
DE Short=AtGH3-3;
GN Name=GH3.3; OrderedLocusNames=At2g23170; ORFNames=T20D16.20;
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 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 [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. 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. {ECO:0000269|PubMed:15659623}.
CC -!- INDUCTION: 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; AC002391; AAB87114.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07424.1; -; Genomic_DNA.
DR EMBL; AY090371; AAL91274.1; -; mRNA.
DR EMBL; BT000823; AAN33198.1; -; mRNA.
DR PIR; T00515; T00515.
DR RefSeq; NP_179898.1; NM_127881.3.
DR AlphaFoldDB; O22190; -.
DR SMR; O22190; -.
DR BioGRID; 2202; 1.
DR STRING; 3702.AT2G23170.1; -.
DR MetOSite; O22190; -.
DR PaxDb; O22190; -.
DR PRIDE; O22190; -.
DR ProteomicsDB; 220749; -.
DR EnsemblPlants; AT2G23170.1; AT2G23170.1; AT2G23170.
DR GeneID; 816849; -.
DR Gramene; AT2G23170.1; AT2G23170.1; AT2G23170.
DR KEGG; ath:AT2G23170; -.
DR Araport; AT2G23170; -.
DR TAIR; locus:2058588; AT2G23170.
DR eggNOG; ENOG502QPMW; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; O22190; -.
DR OMA; KKRPFDP; -.
DR OrthoDB; 374623at2759; -.
DR PhylomeDB; O22190; -.
DR BioCyc; ARA:AT2G23170-MON; -.
DR PRO; PR:O22190; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22190; baseline and differential.
DR Genevisible; O22190; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 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..595
FT /note="Indole-3-acetic acid-amido synthetase GH3.3"
FT /id="PRO_0000203572"
SQ SEQUENCE 595 AA; 67537 MW; 3693E10323AFDD43 CRC64;
MTVDSALRSP MMHSPSTKDV KALRFIEEMT RNVDFVQKKV IREILSRNSD TEYLKRFGLK
GFTDRKTFKT KVPVVIYDDL KPEIQRIANG DRSMILSSYP ITEFLTSSGT SAGERKLMPT
IDEDMDRRQL LYSLLMPVMN LYVPGLDKGK ALYFLFVKTE SKTPGGLPAR PVLTSYYKSE
QFKRRPNDPY NVYTSPNEAI LCPDSSQSMY TQMLCGLLMR HEVLRLGAVF ASGLLRAIGF
LQTNWKELAD DISTGTLSSR ISDPAIKESM SKILTKPDQE LADFITSVCG QDNSWEGIIT
KIWPNTKYLD VIVTGAMAQY IPMLEYYSGG LPMACTMYAS SESYFGINLK PMCKPSEVSY
TIMPNMAYFE FLPHHEVPTE KSELVELADV EVGKEYELVI TTYAGLNRYR VGDILQVTGF
YNSAPQFKFV RRKNVLLSIE SDKTDEAELQ SAVENASLLL GEQGTRVIEY TSYAETKTIP
GHYVIYWELL VKDQTNPPND EVMARCCLEM EESLNSVYRQ SRVADKSIGP LEIRVVKNGT
FEELMDYAIS RGASINQYKV PRCVSFTPIM ELLDSRVVST HFSPALPHWS PERRR
