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GH38_ORYSJ
ID   GH38_ORYSJ              Reviewed;         605 AA.
AC   Q0D4Z6; B9FY76; Q7XIN9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Indole-3-acetic acid-amido synthetase GH3.8 {ECO:0000305};
DE            EC=6.3.2.- {ECO:0000305|PubMed:18192436};
DE   AltName: Full=Auxin-responsive GH3-like protein 8 {ECO:0000303|PubMed:15856348};
DE            Short=OsGH3-8 {ECO:0000303|PubMed:15856348};
DE   AltName: Full=OsMGH3 {ECO:0000303|PubMed:22016342};
GN   Name=GH3.8 {ECO:0000305}; Synonyms=GH3-8 {ECO:0000303|PubMed:18192436};
GN   OrderedLocusNames=Os07g0592600, LOC_Os07g40290;
GN   ORFNames=OJ1710_H11.110, OsJ_023992,
GN   OsJ_24963 {ECO:0000312|EMBL:EEE67513.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16146529; DOI=10.1111/j.1365-313x.2005.02504.x;
RA   Prasad K., Parameswaran S., Vijayraghavan U.;
RT   "OsMADS1, a rice MADS-box factor, controls differentiation of specific cell
RT   types in the lemma and palea and is an early-acting regulator of inner
RT   floral organs.";
RL   Plant J. 43:915-928(2005).
RN   [7]
RP   TISSUE SPECIFICITY, INDUCTION, AND NOMENCLATURE.
RX   PubMed=15856348; DOI=10.1007/s10142-005-0142-5;
RA   Jain M., Kaur N., Tyagi A.K., Khurana J.P.;
RT   "The auxin-responsive GH3 gene family in rice (Oryza sativa).";
RL   Funct. Integr. Genomics 6:36-46(2006).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=18192436; DOI=10.1105/tpc.107.055657;
RA   Ding X., Cao Y., Huang L., Zhao J., Xu C., Li X., Wang S.;
RT   "Activation of the indole-3-acetic acid-amido synthetase GH3-8 suppresses
RT   expansin expression and promotes salicylate- and jasmonate-independent
RT   basal immunity in rice.";
RL   Plant Cell 20:228-240(2008).
RN   [9]
RP   FUNCTION, AND INDUCTION BY AUXIN.
RX   PubMed=22016342; DOI=10.1093/pcp/pcr142;
RA   Yadav S.R., Khanday I., Majhi B.B., Veluthambi K., Vijayraghavan U.;
RT   "Auxin-responsive OsMGH3, a common downstream target of OsMADS1 and
RT   OsMADS6, controls rice floret fertility.";
RL   Plant Cell Physiol. 52:2123-2135(2011).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 6-603 IN COMPLEX WITH AMP.
RX   PubMed=33272567; DOI=10.1016/j.bbrc.2020.11.098;
RA   Xu G., Zhang Y., Li M., Jiao X., Zhou L., Ming Z.;
RT   "Crystal structure of the acyl acid amido synthetase GH3-8 from Oryza
RT   sativa.";
RL   Biochem. Biophys. Res. Commun. 534:266-271(2021).
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 excessive free auxin (PubMed:18192436). Produces more IAA-
CC       Asp levels than IAA-Ala levels in vitro (PubMed:18192436). May
CC       participate in the activation of disease resistance by preventing the
CC       accumulation of free IAA, which reduces the expression of a group of
CC       auxin-responsive genes encoding expansins that control cell wall
CC       loosening and expansion (PubMed:18192436). Contributes to late events
CC       in stamen and carpel differentiation, and influences floret fertility
CC       (PubMed:22016342). {ECO:0000269|PubMed:18192436,
CC       ECO:0000269|PubMed:22016342}.
CC   -!- TISSUE SPECIFICITY: Expressed in the inner floral organs (lodicules,
CC       stamens and carpels) and at lower levels in lemmas and paleas.
CC       {ECO:0000269|PubMed:15856348, ECO:0000269|PubMed:16146529}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at early stage of flower development in
CC       floral meristem and at later stage in lemma, palea and carpel
CC       primordia. {ECO:0000269|PubMed:16146529}.
CC   -!- INDUCTION: Induced by auxin. {ECO:0000269|PubMed:15856348,
CC       ECO:0000269|PubMed:22016342}.
CC   -!- DISRUPTION PHENOTYPE: Slight increase in disease susceptibility to
CC       Xanthomonas oryzae pv oryzae. {ECO:0000269|PubMed:18192436}.
CC   -!- MISCELLANEOUS: Plants overexpressing GH3-8 exhibit enhanced disease
CC       resistance to Xanthomonas oryzae pv oryzae (PubMed:18192436). Plants
CC       overexpressing GH3-8 exhibit abnormal morphology and dwarf phenotype
CC       (PubMed:18192436, PubMed:22016342). Plants silencing GH3-8 produce
CC       mostly non-viable pollen grains (PubMed:22016342).
CC       {ECO:0000269|PubMed:18192436, ECO:0000269|PubMed:22016342}.
CC   -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AP003846; BAC79627.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAF22077.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT02451.1; -; Genomic_DNA.
DR   EMBL; CM000144; EEE67513.1; -; Genomic_DNA.
DR   EMBL; AK101193; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015647797.1; XM_015792311.1.
DR   PDB; 7DK8; X-ray; 1.99 A; A=6-603.
DR   PDBsum; 7DK8; -.
DR   AlphaFoldDB; Q0D4Z6; -.
DR   SMR; Q0D4Z6; -.
DR   STRING; 4530.OS07T0592600-01; -.
DR   PaxDb; Q0D4Z6; -.
DR   PRIDE; Q0D4Z6; -.
DR   EnsemblPlants; Os07t0592600-01; Os07t0592600-01; Os07g0592600.
DR   GeneID; 4343785; -.
DR   Gramene; Os07t0592600-01; Os07t0592600-01; Os07g0592600.
DR   KEGG; osa:4343785; -.
DR   eggNOG; ENOG502QR80; Eukaryota.
DR   HOGENOM; CLU_016249_2_1_1; -.
DR   InParanoid; Q0D4Z6; -.
DR   OMA; EGFFAIQ; -.
DR   OrthoDB; 374623at2759; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000007752; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   Genevisible; Q0D4Z6; OS.
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:0016208; F:AMP binding; IDA:UniProtKB.
DR   GO; GO:0010279; F:indole-3-acetic acid amido synthetase activity; IDA:UniProtKB.
DR   GO; GO:0010252; P:auxin homeostasis; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR   GO; GO:1900424; P:regulation of defense response to bacterium; IMP:UniProtKB.
DR   InterPro; IPR004993; GH3.
DR   PANTHER; PTHR31901; PTHR31901; 1.
DR   Pfam; PF03321; GH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ligase; Plant defense; Reference proteome.
FT   CHAIN           1..605
FT                   /note="Indole-3-acetic acid-amido synthetase GH3.8"
FT                   /id="PRO_0000203585"
FT   BINDING         115
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:33272567,
FT                   ECO:0007744|PDB:7DK8"
FT   BINDING         342..346
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:33272567,
FT                   ECO:0007744|PDB:7DK8"
FT   BINDING         365
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:33272567,
FT                   ECO:0007744|PDB:7DK8"
FT   BINDING         421
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:33272567,
FT                   ECO:0007744|PDB:7DK8"
FT   BINDING         440
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:33272567,
FT                   ECO:0007744|PDB:7DK8"
FT   CONFLICT        292
FT                   /note="R -> S (in Ref. 5; AK101193)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   605 AA;  66932 MW;  F8F8035441FFA3B2 CRC64;
     MAVMTDVSTT GTALRTPAAG AVKEGDVEKL RFIDEMTTNV DAVQERVLGE ILGRNAGTEY
     LTKCGLDGAT DRAAFRAKVP VVSYDDLQPY IQRIANGDRS PILSTHPVSE FLTSSGTSAG
     ERKLMPTIMD ELDRRQLLYS LLMPVMNLYV PGLDKGKGLY FLFVKSETKT PGGLTARPVL
     TSYYKSDHFK NRPYDPYHNY TSPTAAILCA DAFQSMYAQM VCGLCQRNDV LRLGAVFASG
     LLRAIRFLQL NWEQLADDIE SGELTPRVTD PSVREAVAAI LLPDPELAKL IRAECSKGDW
     AGIITRVWPN TKYLDVIVTG AMAQYIPTLE FYSGGLPMAC TMYASSECYF GLNLRPMCDP
     SEVSYTIMPN MGYFEFLPVD ETGAASGDAT QLVDLARVEV GREYELVITT YAGLNRYRVG
     DVLRVTGFHN AAPQFRFVRR KNVLLSIESD KTDEAELQRA VERASALLRP HGASVVEYTS
     QACTKRIPGH YVIYWELLTK GAGATVVDAD TLGRCCLEME EALNTVYRQS RVADGSIGPL
     EIRVVRPGTF EELMDYAISR GASINQYKVP RCVTFPPIVE LLDSRVVSSH FSPALPHWTP
     ARRSE
 
 
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