GH35_ARATH
ID GH35_ARATH Reviewed; 612 AA.
AC O81829;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Indole-3-acetic acid-amido synthetase GH3.5;
DE EC=6.3.2.-;
DE AltName: Full=Auxin-responsive GH3-like protein 5;
DE Short=AtGH3-5;
GN Name=GH3.5; OrderedLocusNames=At4g27260; ORFNames=M4I22.70;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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; AL030978; CAA19720.1; -; Genomic_DNA.
DR EMBL; AL161566; CAB79581.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85318.1; -; Genomic_DNA.
DR EMBL; AY070038; AAL49795.1; -; mRNA.
DR EMBL; AY096516; AAM20166.1; -; mRNA.
DR PIR; T05750; T05750.
DR RefSeq; NP_194456.1; NM_118860.5.
DR PDB; 5KOD; X-ray; 2.20 A; A/B/C/D=1-612.
DR PDBsum; 5KOD; -.
DR AlphaFoldDB; O81829; -.
DR SMR; O81829; -.
DR BioGRID; 14121; 1.
DR STRING; 3702.AT4G27260.1; -.
DR PaxDb; O81829; -.
DR PRIDE; O81829; -.
DR ProteomicsDB; 220751; -.
DR EnsemblPlants; AT4G27260.1; AT4G27260.1; AT4G27260.
DR GeneID; 828834; -.
DR Gramene; AT4G27260.1; AT4G27260.1; AT4G27260.
DR KEGG; ath:AT4G27260; -.
DR Araport; AT4G27260; -.
DR TAIR; locus:2131739; AT4G27260.
DR eggNOG; ENOG502QQAN; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; O81829; -.
DR OMA; PRCVNYA; -.
DR OrthoDB; 374623at2759; -.
DR PhylomeDB; O81829; -.
DR BioCyc; ARA:AT4G27260-MON; -.
DR BioCyc; MetaCyc:AT4G27260-MON; -.
DR PRO; PR:O81829; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81829; baseline and differential.
DR Genevisible; O81829; 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 GO; GO:0010120; P:camalexin biosynthetic process; IMP:TAIR.
DR GO; GO:1901183; P:positive regulation of camalexin biosynthetic process; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR InterPro; IPR004993; GH3.
DR PANTHER; PTHR31901; PTHR31901; 1.
DR Pfam; PF03321; GH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ligase; Reference proteome.
FT CHAIN 1..612
FT /note="Indole-3-acetic acid-amido synthetase GH3.5"
FT /id="PRO_0000203574"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:5KOD"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 233..256
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 315..320
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 422..435
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 460..471
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 472..477
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 479..489
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 496..505
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 513..526
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 529..536
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 545..549
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 553..563
FT /evidence="ECO:0007829|PDB:5KOD"
FT HELIX 580..587
FT /evidence="ECO:0007829|PDB:5KOD"
FT STRAND 590..595
FT /evidence="ECO:0007829|PDB:5KOD"
SQ SEQUENCE 612 AA; 69283 MW; 8E0F91FE7EE2725A CRC64;
MPEAPKKESL EVFDLTLDQK NKQKLQLIEE LTSNADQVQR QVLEEILTRN ADVEYLRRHD
LNGRTDRETF KNIMPVITYE DIEPEINRIA NGDKSPILSS KPISEFLTSS GTSGGERKLM
PTIEEELDRR SLLYSLLMPV MSQFVPGLEN GKGMYFLFIK SESKTPGGLP ARPVLTSYYK
SSHFKERPYD PYTNYTSPNE TILCSDSYQS MYSQMLCGLC QHQEVLRVGA VFASGFIRAI
KFLEKHWIEL VRDIRTGTLS SLITDPSVRE AVAKILKPSP KLADFVEFEC KKSSWQGIIT
RLWPNTKYVD VIVTGTMSQY IPTLDYYSNG LPLVCTMYAS SECYFGVNLR PLCKPSEVSY
TLIPSMAYFE FLPVHRNNGV TNSINLPKAL TEKEQQELVD LVDVKLGQEY ELVVTTYAGL
CRYRVGDLLR VTGFKNKAPQ FSFICRKNVV LSIDSDKTDE VELQNAVKNA VTHLVPFDAS
LSEYTSYADT SSIPGHYVLF WELCLDGNTP IPPSVFEDCC LAVEESFNTV YRQGRVSDKS
IGPLEIKIVE PGTFDKLMDY AISLGASINQ YKTPRCVKFA PIIELLNSRV VDSYFSPKCP
KWVPGHKQWG SN
