ID   IAAL_PSESS              Reviewed;         395 AA.
AC   P18204;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Indoleacetate--lysine synthetase;
DE            EC=6.3.2.20;
DE   AltName: Full=IAA-lysine synthetase;
DE   AltName: Full=Indoleacetate--lysine ligase;
DE   AltName: Full=N-(Indole-3-acetyl)-L-lysine synthetase;
GN   Name=iaaL;
OS   Pseudomonas savastanoi (Pseudomonas syringae pv. savastanoi).
OG   Plasmid pIAA1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=29438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EW2009;
RX   PubMed=2377619; DOI=10.1073/pnas.87.15.5797;
RA   Roberto F., Klee H., White F., Nordeen R., Kosuge T.;
RT   "Expression and fine structure of the gene encoding N epsilon-(indole-3-
RT   acetyl)-L-lysine synthetase from Pseudomonas savastanoi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5797-5801(1990).
CC   -!- FUNCTION: Conversion of IAA to IAA-lysine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(indol-3-yl)acetate + ATP + L-lysine = ADP + H(+) + N(6)-
CC         [(indole-3-yl)acetyl]-L-lysine + phosphate; Xref=Rhea:RHEA:14857,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:30854,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58105,
CC         ChEBI:CHEBI:456216; EC=6.3.2.20;
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; M35373; AAA25850.1; -; Genomic_DNA.
DR   PIR; A35961; A35961.
DR   AlphaFoldDB; P18204; -.
DR   SMR; P18204; -.
DR   KEGG; ag:AAA25850; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047721; F:indoleacetate-lysine synthetase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Auxin biosynthesis; Ligase; Nucleotide-binding; Plasmid.
FT   CHAIN           1..395
FT                   /note="Indoleacetate--lysine synthetase"
FT                   /id="PRO_0000193102"
SQ   SEQUENCE   395 AA;  44624 MW;  7184F400B68C7B99 CRC64;
     MTAYDMEKEW SRISITAAKI HQNNDFEGFT YQDFRTHVPI MDKDGFAAQT ERCLERNERN
     CLIGFTSGTS GNIKRCYYYY DCEVDEDSSL SNVFRSNGFI LPGDRCANLF TINLFSALNN
     TITMMAGNCG AHVVSVGDIT LVTKSHFEAL NSIKLNVLLG VPSTILQFIN AMQHNGVHIN
     IEKVVFTGES LKTFQKKIIR QAFGEQVSIV GVYGSSEGGI LGFTNSPCHT EYEFLSDKYF
     IEKEGDSILI TSLTRENFTP LLRYRLGDTA TLSMKGDKLY LTDIQREDMS FNFMGNLIGL
     GIIQQTIKQT LGRSLEIQVH LSVTEERKEL VTVFVQASEV DEDERVRIET AIADIPDIKE
     AYQKNQGTVS VLRKDARDYA VSERGKMLYI IDRRN