GH315_ARATH
ID GH315_ARATH Reviewed; 595 AA.
AC Q8GZ29; Q9LYR9;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Indole-3-acetic acid-amido synthetase GH3.15 {ECO:0000303|PubMed:12036261};
DE EC=6.3.2.- {ECO:0000269|PubMed:29462792, ECO:0000269|PubMed:30315112};
DE AltName: Full=Auxin-responsive GH3-like protein 15 {ECO:0000303|PubMed:12036261};
DE Short=AtGH3-15 {ECO:0000303|PubMed:12036261};
DE AltName: Full=Protein GRETCHEN HAGEN 3.15 {ECO:0000303|PubMed:12036261};
GN Name=GH3.15 {ECO:0000303|PubMed:12036261};
GN OrderedLocusNames=At5g13370 {ECO:0000312|Araport:AT5G13370};
GN ORFNames=T22N19.20 {ECO:0000312|EMBL:CAB87144.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH AMP, CATALYTIC
RP ACTIVITY, DISULFIDE BONDS, FUNCTION, MUTAGENESIS OF SER-122; MET-162;
RP PHE-166 AND PHE-332, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=29462792; DOI=10.1074/jbc.ra118.002006;
RA Sherp A.M., Westfall C.S., Alvarez S., Jez J.M.;
RT "Arabidopsis thaliana GH3.15 acyl acid amido synthetase has a highly
RT specific substrate preference for the auxin precursor indole-3-butyric
RT acid.";
RL J. Biol. Chem. 293:4277-4288(2018).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH
RP 4-(2,4-DICHLOROPHENOXY)BUTYRIC ACID, CATALYTIC ACTIVITY, FUNCTION,
RP DISRUPTION PHENOTYPE, DISULFIDE BONDS, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=30315112; DOI=10.1074/jbc.ra118.004975;
RA Sherp A.M., Lee S.G., Schraft E., Jez J.M.;
RT "Modification of auxinic phenoxyalkanoic acid herbicides by the acyl acid
RT amido synthetase GH3.15 from Arabidopsis.";
RL J. Biol. Chem. 293:17731-17738(2018).
CC -!- FUNCTION: Indole-3-acetic acid-amido (IAA) synthetase that catalyzes
CC the conjugation of amino acids to auxin specifically using the auxin
CC precursor indole-3-butyric acid (IBA) and glutamine and, possibly,
CC cysteine as substrates (PubMed:29462792, PubMed:30315112). Displays
CC high catalytic activity with the auxinic phenoxyalkanoic acid
CC herbicides 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB) and to some
CC extent 2,4-dichlorophenoxylacetic acid (2,4-D) as substrates, thus
CC confering resistance to herbicides (PubMed:30315112).
CC {ECO:0000269|PubMed:29462792, ECO:0000269|PubMed:30315112}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(indol-3-yl)butanoate + ATP + L-cysteine = (indol-3-
CC yl)butanoyl-L-cysteine + AMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:59876, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:35235, ChEBI:CHEBI:143274,
CC ChEBI:CHEBI:143280, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:29462792};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(indol-3-yl)butanoate + ATP + L-glutamine = (indol-3-
CC yl)butanoyl-L-glutamine + AMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:59864, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58359, ChEBI:CHEBI:143274,
CC ChEBI:CHEBI:143275, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:29462792, ECO:0000269|PubMed:30315112};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(2,4-dichlorophenoxy)butanoate + ATP + L-glutamine = 4-(2,4-
CC dichlorophenoxy)butanoyl-L-glutamine + AMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:59868, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58359, ChEBI:CHEBI:143277,
CC ChEBI:CHEBI:143278, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:30315112};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=556 uM for indole-3-acetic acid (in the presence of ATP and
CC glutamine) {ECO:0000269|PubMed:29462792,
CC ECO:0000269|PubMed:30315112};
CC KM=3430 uM for indole-3-propionic acid (in the presence of ATP and
CC glutamine) {ECO:0000269|PubMed:29462792};
CC KM=527 uM for indole-3-butyric acid (in the presence of ATP and
CC glutamine) {ECO:0000269|PubMed:29462792,
CC ECO:0000269|PubMed:30315112};
CC KM=1120 uM for jasmonic acid (in the presence of ATP and glutamine)
CC {ECO:0000269|PubMed:29462792};
CC KM=1780 uM for glutamine (in the presence of ATP and indole-3-butyric
CC acid) {ECO:0000269|PubMed:29462792};
CC KM=2530 uM for glutamine (in the presence of ATP and jasmonic acid)
CC {ECO:0000269|PubMed:29462792};
CC KM=2080 uM for cysteine (in the presence of ATP and indole-3-butyric
CC acid) {ECO:0000269|PubMed:29462792};
CC KM=12300 uM for histidine (in the presence of ATP and indole-3-
CC butyric acid) {ECO:0000269|PubMed:29462792};
CC KM=5670 uM for methionine (in the presence of ATP and indole-3-
CC butyric acid) {ECO:0000269|PubMed:29462792};
CC KM=18600 uM for tyrosine (in the presence of ATP and indole-3-butyric
CC acid) {ECO:0000269|PubMed:29462792};
CC KM=84 uM for ATP (in the presence of glutamine and indole-3-butyric
CC acid) {ECO:0000269|PubMed:29462792};
CC KM=590 uM for 4-(2,4-dichlorophenoxy)butyric acid (in the presence of
CC ATP and glutamine) {ECO:0000269|PubMed:30315112};
CC KM=3790 uM for 2,4-dichlorophenoxylacetic acid (in the presence of
CC ATP and glutamine) {ECO:0000269|PubMed:30315112};
CC KM=970 uM for glutamine (in the presence of ATP and 4-(2,4-
CC dichlorophenoxy)butyric acid) {ECO:0000269|PubMed:30315112};
CC KM=7240 uM for cysteine (in the presence of ATP and 4-(2,4-
CC dichlorophenoxy)butyric acid) {ECO:0000269|PubMed:30315112};
CC KM=9290 uM for histidine (in the presence of ATP and 4-(2,4-
CC dichlorophenoxy)butyric acid) {ECO:0000269|PubMed:30315112};
CC KM=10600 uM for methionine (in the presence of ATP and 4-(2,4-
CC dichlorophenoxy)butyric acid) {ECO:0000269|PubMed:30315112};
CC KM=18400 uM for tyrosine (in the presence of ATP and 4-(2,4-
CC dichlorophenoxy)butyric acid) {ECO:0000269|PubMed:30315112};
CC KM=23200 uM for 2,4,5-trichlorophenoxyacetic acid (in the presence of
CC ATP and glutamine) {ECO:0000269|PubMed:30315112};
CC KM=1130 uM for 4-(4-chloro-2-methylphenoxy)butanoic acid (in the
CC presence of ATP and glutamine) {ECO:0000269|PubMed:30315112};
CC KM=3550 uM for 4-(2-chlorophenoxy)butanoic acid (in the presence of
CC ATP and glutamine) {ECO:0000269|PubMed:30315112};
CC KM=180 uM for 4-(2,6-dimethylphenoxy)butanoic acid (in the presence
CC of ATP and glutamine) {ECO:0000269|PubMed:30315112};
CC KM=14800 uM for 4-(4-methoxyphenoxy)butanoic acid (in the presence of
CC ATP and glutamine) {ECO:0000269|PubMed:30315112};
CC KM=2140 uM for 4-phenoxybutyric acid (in the presence of ATP and
CC glutamine) {ECO:0000269|PubMed:30315112};
CC KM=6000 uM for 4-phenylbutryic acid (in the presence of ATP and
CC glutamine) {ECO:0000269|PubMed:30315112};
CC KM=960 uM for 5-phenylvaleric acid (in the presence of ATP and
CC glutamine) {ECO:0000269|PubMed:30315112};
CC KM=680 uM for 5-(4-fluorophenyl)valeric acid (in the presence of ATP
CC and glutamine) {ECO:0000269|PubMed:30315112};
CC Note=kcat is 0.76 min(-1) with indole-3-acetic acid as substrate (in
CC the presence of ATP and glutamine) (PubMed:29462792,
CC PubMed:30315112). kcat is 10.2 min(-1) with indole-3-propionic acid
CC as substrate (in the presence of ATP and glutamine)
CC (PubMed:29462792). kcat is 9.9 min(-1) with indole-3-butyric acid as
CC substrate (in the presence of ATP and glutamine) (PubMed:29462792,
CC PubMed:30315112). kcat is 4.4 min(-1) with jasmonic acid as substrate
CC (in the presence of ATP and glutamine) (PubMed:29462792). kcat is 17
CC min(-1) with glutamine as substrate (in the presence of ATP and
CC indole-3-butyric acid) (PubMed:29462792). kcat is 4 min(-1) with
CC glutamine as substrate (in the presence of ATP and jasmonic acid)
CC (PubMed:29462792). kcat is 16 min(-1) with cysteine as substrate (in
CC the presence of ATP and indole-3-butyric acid) (PubMed:29462792).
CC kcat is 21 min(-1) with histidine as substrate (in the presence of
CC ATP and indole-3-butyric acid) (PubMed:29462792). kcat is 13 min(-1)
CC with methionine as substrate (in the presence of ATP and indole-3-
CC butyric acid) (PubMed:29462792). kcat is 25 min(-1) with tyrosine as
CC substrate (in the presence of ATP and indole-3-butyric acid)
CC (PubMed:29462792). kcat is 13 min(-1) with ATP as substrate (in the
CC presence of indole-3-butyric acid and glutamine) (PubMed:29462792).
CC kcat is 11 min(-1) with 4-(2,4-dichlorophenoxy)butyric acid as
CC substrate (in the presence of ATP and glutamine) (PubMed:30315112).
CC kcat is 1.3 min(-1) with 2,4-dichlorophenoxylacetic acid as substrate
CC (in the presence of ATP and glutamine) (PubMed:30315112). kcat is
CC 52.3 min(-1) with glutamine as substrate (in the presence of ATP and
CC 4-(2,4-dichlorophenoxy)butyric acid) (PubMed:30315112). kcat is 52.5
CC min(-1) with cysteine as substrate (in the presence of ATP and 4-
CC (2,4-dichlorophenoxy)butyric acid) (PubMed:30315112). kcat is 43.1
CC min(-1) with histidine as substrate (in the presence of ATP and 4-
CC (2,4-dichlorophenoxy)butyric acid) (PubMed:30315112). kcat is 27.5
CC min(-1) with methionine as substrate (in the presence of ATP and 4-
CC (2,4-dichlorophenoxy)butyric acid) (PubMed:30315112). kcat is 12
CC min(-1) with tyrosine as substrate (in the presence of ATP and 4-
CC (2,4-dichlorophenoxy)butyric acid) (PubMed:30315112). kcat is 4.3
CC min(-1) with 2,4,5-trichlorophenoxyacetic acid as substrate (in the
CC presence of ATP and glutamine) (PubMed:30315112). kcat is 15.6 min(-
CC 1) with 4-(4-chloro-2-methylphenoxy)butanoic acid as substrate (in
CC the presence of ATP and glutamine) (PubMed:30315112). kcat is 24
CC min(-1) with 4-(2-chlorophenoxy)butanoic acid as substrate (in the
CC presence of ATP and glutamine) (PubMed:30315112). kcat is 5.4 min(-1)
CC with 4-(2,6-dimethylphenoxy)butanoic acid as substrate (in the
CC presence of ATP and glutamine) (PubMed:30315112). kcat is 29.8 min(-
CC 1) with 4-(4-methoxyphenoxy)butanoic acid as substrate (in the
CC presence of ATP and glutamine) (PubMed:30315112). kcat is 16.2 min(-
CC 1) with 4-phenoxybutyric acid as substrate (in the presence of ATP
CC and glutamine) (PubMed:30315112). kcat is 15 min(-1) with 4-
CC phenylbutryic acid as substrate (in the presence of ATP and
CC glutamine) (PubMed:30315112). kcat is 26.6 min(-1) with 5-
CC phenylvaleric acid as substrate (in the presence of ATP and
CC glutamine) (PubMed:30315112). kcat is 24 min(-1) with 5-(4-
CC fluorophenyl)valeric acid as substrate (in the presence of ATP and
CC glutamine) (PubMed:30315112). {ECO:0000269|PubMed:29462792,
CC ECO:0000269|PubMed:30315112};
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, and parts of the
CC siliques. {ECO:0000269|PubMed:29462792}.
CC -!- DEVELOPMENTAL STAGE: Expressed widely in young seedling, including
CC roots, shoots, and cotyledons. In older seedlings, present the primary
CC root, shoots, and cotyledons, but not in the root epidermal cells or
CC root hairs. Later observed in the cotyledons and the shoots, but not in
CC the true leaves. In adult plants, accumulates in the primary root and
CC lateral root tips and in the roots near the root/shoot junction. In
CC mature siliques, confined to the tip of the silique in the style just
CC below the stigma and at the base of the silique in the replum and
CC abscission zone of siliques. {ECO:0000269|PubMed:29462792}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in normal conditions
CC (PubMed:29462792). Slight reduction in root length when grown on media
CC containing indole-3-butyric acid (IBA) (PubMed:29462792).
CC Hypersensitivity to the auxinic phenoxyalkanoic acid herbicide 4-(2,4-
CC dichlorophenoxy)butyric acid (2,4-DB) (PubMed:30315112).
CC {ECO:0000269|PubMed:29462792, ECO:0000269|PubMed:30315112}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87144.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163572; CAB87144.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91887.1; -; Genomic_DNA.
DR EMBL; BT005922; AAO64857.1; -; mRNA.
DR EMBL; AK117242; BAC41918.1; -; mRNA.
DR PIR; T48584; T48584.
DR RefSeq; NP_196841.2; NM_121340.3.
DR PDB; 6AVH; X-ray; 3.01 A; A/B/C/D=1-595.
DR PDB; 6E1Q; X-ray; 2.15 A; A=1-595.
DR PDBsum; 6AVH; -.
DR PDBsum; 6E1Q; -.
DR AlphaFoldDB; Q8GZ29; -.
DR SMR; Q8GZ29; -.
DR STRING; 3702.AT5G13370.1; -.
DR PaxDb; Q8GZ29; -.
DR PRIDE; Q8GZ29; -.
DR ProteomicsDB; 179737; -.
DR EnsemblPlants; AT5G13370.1; AT5G13370.1; AT5G13370.
DR GeneID; 831178; -.
DR Gramene; AT5G13370.1; AT5G13370.1; AT5G13370.
DR KEGG; ath:AT5G13370; -.
DR Araport; AT5G13370; -.
DR TAIR; locus:2181630; AT5G13370.
DR eggNOG; ENOG502QPMU; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; Q8GZ29; -.
DR OMA; EPSDIIC; -.
DR OrthoDB; 374623at2759; -.
DR PhylomeDB; Q8GZ29; -.
DR PRO; PR:Q8GZ29; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GZ29; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070406; F:glutamine binding; IDA:TAIR.
DR GO; GO:0010249; P:auxin conjugate metabolic process; IDA:TAIR.
DR InterPro; IPR004993; GH3.
DR PANTHER; PTHR31901; PTHR31901; 1.
DR Pfam; PF03321; GH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..595
FT /note="Indole-3-acetic acid-amido synthetase GH3.15"
FT /id="PRO_0000447233"
FT BINDING 97..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29462792,
FT ECO:0007744|PDB:6AVH"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29462792,
FT ECO:0007744|PDB:6AVH"
FT BINDING 325..330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29462792,
FT ECO:0007744|PDB:6AVH"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30315112,
FT ECO:0007744|PDB:6E1Q"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30315112,
FT ECO:0007744|PDB:6E1Q"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29462792,
FT ECO:0007744|PDB:6AVH"
FT BINDING 408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29462792,
FT ECO:0007744|PDB:6AVH"
FT MUTAGEN 122
FT /note="S->F,I,L: Increased affinity and enhanced catalytic
FT activity leading to improved efficiency toward indole-3-
FT butyric acid. Reduced affinity but increased catalytic
FT activity leading to almost unaffected efficiency toward
FT indole-3-acetic acid."
FT /evidence="ECO:0000269|PubMed:29462792"
FT MUTAGEN 122
FT /note="S->W: Reduced affinity and altered catalytic
FT activity leading to decreased efficiency toward indole-3-
FT butyric acid."
FT /evidence="ECO:0000269|PubMed:29462792"
FT MUTAGEN 122
FT /note="S->Y: Reduced affinity but enhanced catalytic
FT activity leading to improved efficiency toward indole-3-
FT butyric acid. Reduced affinity but increased catalytic
FT activity leading to almost unaffected efficiency toward
FT indole-3-acetic acid."
FT /evidence="ECO:0000269|PubMed:29462792"
FT MUTAGEN 162
FT /note="M->V: Increased affinity and enhanced catalytic
FT activity leading to improved efficiency toward indole-3-
FT butyric acid. Slightly increased affinity but normal
FT catalytic activity leading to slightly improved efficiency
FT toward indole-3-acetic acid."
FT /evidence="ECO:0000269|PubMed:29462792"
FT MUTAGEN 166
FT /note="F->V: Strongly reduced affinity but enhanced
FT catalytic activity leading to reduced efficiency toward
FT indole-3-butyric acid. Slightly increased affinity and
FT slightly better catalytic activity leading to slightly
FT improved efficiency toward indole-3-acetic acid."
FT /evidence="ECO:0000269|PubMed:29462792"
FT MUTAGEN 332
FT /note="F->V: Strongly reduced affinity but normal catalytic
FT activity leading to reduced efficiency toward indole-3-
FT butyric acid. Strongly reduced affinity and slightly better
FT catalytic activity leading to reduced efficiency toward
FT indole-3-acetic acid."
FT /evidence="ECO:0000269|PubMed:29462792"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 24..38
FT /evidence="ECO:0007829|PDB:6E1Q"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 91..111
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 112..132
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6AVH"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6E1Q"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 220..243
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 309..316
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 408..416
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 419..427
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 441..452
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 453..458
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 461..470
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 472..485
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 497..510
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 513..520
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:6E1Q"
FT HELIX 537..547
FT /evidence="ECO:0007829|PDB:6E1Q"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:6AVH"
FT HELIX 564..571
FT /evidence="ECO:0007829|PDB:6E1Q"
FT STRAND 574..579
FT /evidence="ECO:0007829|PDB:6E1Q"
SQ SEQUENCE 595 AA; 66979 MW; 510294E9B2F5D1B1 CRC64;
MLPKFDPTNQ KACLSLLEDL TTNVKQIQDS VLEAILSRNA QTEYLRGFLN GQVDKQNFKK
NVPVVTYEDI RSYIDRIANG EPSDLICDRP ISVLLTSSGT SGGVPKLIPL TTEDLEQRIS
FSSLYAPLLY KHIDGLSEGK SLIFYFVTRE SKTANGLMVR TMVTSFLKSI KQTNSFLWDS
LQVSPHAITT CADTTQSMYC QLLCGLLERD NVARLGAPFA SSFLKVIKFL EDHWPELCSN
IRTGRLSDWI TDATCTSGIG KFLTAPNPEL ASLIEQECSK TSWEAILKRL WPKAKCIESI
ITGTMAQYIP LLEFYSGGLP LTSSFYGSSE CFMGVNFNPL CKPSDVSYTI IPCMGYFEFL
EVEKDHQEAG HDPTEKPVVV DLVDVKIGHD YEPVVTTFSG LYRYRVGDVL RATGFYNNAP
HFCFVGRQKV VLSIDMDKTY EDDLLKAVTN AKLLLEPHDL MLMDFTSRVD SSSFPGHYVI
YWELGSKVKD AKFEPNRDVM EECCFTVEES LDAVYRKGRK NDKNIGPLEI KVVKPGAFDE
LMNFFLSRGS SVSQYKTPRS VTNEEALKIL EANVISEFLS RKIPSWELHE LHSGR
