GH34_ARATH
ID GH34_ARATH Reviewed; 597 AA.
AC Q9LQ68;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Indole-3-acetic acid-amido synthetase GH3.4;
DE EC=6.3.2.-;
DE AltName: Full=Auxin-responsive GH3-like protein 4;
DE Short=AtGH3-4;
DE AltName: Full=CF4-like protein;
GN Name=GH3.4; OrderedLocusNames=At1g59500; ORFNames=T30E16.2, T4M14.15;
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=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 [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 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 [4]
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; AB076984; BAB82427.1; -; Genomic_DNA.
DR EMBL; AC009317; AAF79776.1; -; Genomic_DNA.
DR EMBL; AC027036; AAK62800.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33579.1; -; Genomic_DNA.
DR RefSeq; NP_176159.1; NM_104643.1.
DR AlphaFoldDB; Q9LQ68; -.
DR SMR; Q9LQ68; -.
DR STRING; 3702.AT1G59500.1; -.
DR PaxDb; Q9LQ68; -.
DR PRIDE; Q9LQ68; -.
DR ProteomicsDB; 220750; -.
DR EnsemblPlants; AT1G59500.1; AT1G59500.1; AT1G59500.
DR GeneID; 842240; -.
DR Gramene; AT1G59500.1; AT1G59500.1; AT1G59500.
DR KEGG; ath:AT1G59500; -.
DR Araport; AT1G59500; -.
DR TAIR; locus:2202832; AT1G59500.
DR eggNOG; ENOG502QR80; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; Q9LQ68; -.
DR OMA; SHPINEF; -.
DR OrthoDB; 374623at2759; -.
DR PhylomeDB; Q9LQ68; -.
DR BioCyc; ARA:AT1G59500-MON; -.
DR BioCyc; MetaCyc:AT1G59500-MON; -.
DR PRO; PR:Q9LQ68; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQ68; baseline and differential.
DR Genevisible; Q9LQ68; 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..597
FT /note="Indole-3-acetic acid-amido synthetase GH3.4"
FT /id="PRO_0000203573"
SQ SEQUENCE 597 AA; 67046 MW; FCDFCFCA23A2A7C8 CRC64;
MAVDSLLQSG MASPTTSETE VKALKFIEEI TRNPDSVQEK VLGEILSRNS NTEYLKRFDL
NGAVDRKSFK SKVPVVIYED LKTDIQRISN GDRSPILSSH PITEFLTSSG TSAGERKLMP
TIEEDINRRQ LLGNLLMPVM NLYVPGLDKG KGLYFLFVKS ESTTSGGLPA RPALTSYYKS
DYFRTSDSDS VYTSPKEAIL CCDSSQSMYT QMLCGLLMRH EVNRLGAVFP SGLLRAISFL
QNNWKELSQD ISTGTLSSKI FDHAIKTRMS NILNKPDQEL AEFLIGVCSQ ENWEGIITKI
WPNTKYLDVI VTGAMAEYIP MLEYYSGGLP MASMIYASSE SYFGINLNPM CKPSEVSYTI
FPNMAYFEFL PHNHDGDGGV EATSLVELAD VEVGKEYELV ITTYAGLYRY RVGDILRVTG
FHNSAPQFKF IRRENVLLSI ESDKTDEADL QKAVENASRL LAEQGTRVIE YTSYADTKTI
PGHYVIYWEL LSRDQSNALP SDEVMAKCCL EMEESLNAVY RQSRVSDKSI GPLEIRVVQN
GTFEELMDFS ISRGSSINQY KVPRCVSLTP IMKLLDSRVV SAHFSPSLPH WSPERRH
