ID   IUCA_ECOLX              Reviewed;         575 AA.
AC   Q47316;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=N(2)-citryl-N(6)-acetyl-N(6)-hydroxylysine synthase;
DE            EC=6.3.2.38;
DE   AltName: Full=Aerobactin synthase IucA;
GN   Name=iucA;
OS   Escherichia coli.
OG   Plasmid IncFI ColV3-K30.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8003107; DOI=10.1006/jmbi.1994.1290;
RA   Martinez J.L., Herrero M., de Lorenzo V.;
RT   "The organization of intercistronic regions of the aerobactin operon of
RT   pColV-K30 may account for the differential expression of the iucABCD iutA
RT   genes.";
RL   J. Mol. Biol. 238:288-293(1994).
RN   [2]
RP   FUNCTION IN AEROBACTIN BIOSYNTHESIS, AND NOMENCLATURE.
RX   PubMed=2935523; DOI=10.1128/jb.165.2.570-578.1986;
RA   de Lorenzo V., Bindereif A., Paw B.H., Neilands J.B.;
RT   "Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 165:570-578(1986).
RN   [3]
RP   FUNCTION IN AEROBACTIN BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RX   PubMed=3087960; DOI=10.1128/jb.167.1.350-355.1986;
RA   de Lorenzo V., Neilands J.B.;
RT   "Characterization of iucA and iucC genes of the aerobactin system of
RT   plasmid ColV-K30 in Escherichia coli.";
RL   J. Bacteriol. 167:350-355(1986).
CC   -!- FUNCTION: Catalyzes the attachment of a first N-acetyl-N-hydroxylysine
CC       to a carboxylic group of citric acid to yield N-citryl-N-acetyl-N-
CC       hydroxylysine. Involved in the biosynthesis of the siderophore
CC       aerobactin which is a chelator that mediates the high-affinity iron
CC       transport systems induced under iron-stressed conditions.
CC       {ECO:0000269|PubMed:2935523, ECO:0000269|PubMed:3087960}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + citrate + N(6)-acetyl-N(6)-hydroxy-L-lysine = AMP +
CC         diphosphate + H(+) + N(2)-citryl-N(6)-acetyl-N(6)-hydroxy-L-lysine;
CC         Xref=Rhea:RHEA:32163, ChEBI:CHEBI:15378, ChEBI:CHEBI:16947,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58122,
CC         ChEBI:CHEBI:63796, ChEBI:CHEBI:456215; EC=6.3.2.38;
CC   -!- PATHWAY: Siderophore biosynthesis; aerobactin biosynthesis.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not able to produce
CC       aerobactin and accumulate N-acetyl-N-hydroxylysine.
CC       {ECO:0000269|PubMed:3087960}.
CC   -!- SIMILARITY: Belongs to the IucA/IucC family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X76100; CAA53707.1; -; Genomic_DNA.
DR   PIR; S44018; S44018.
DR   AlphaFoldDB; Q47316; -.
DR   SMR; Q47316; -.
DR   PRIDE; Q47316; -.
DR   KEGG; ag:CAA53707; -.
DR   BioCyc; MetaCyc:MON-11597; -.
DR   BRENDA; 6.3.2.38; 2026.
DR   UniPathway; UPA00014; -.
DR   GO; GO:0050565; F:aerobactin synthase activity; IMP:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019270; P:aerobactin biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0055072; P:iron ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR   InterPro; IPR007310; Aerobactin_biosyn_IucA/IucC_N.
DR   InterPro; IPR022770; FhuF_domain.
DR   InterPro; IPR037455; LucA/IucC-like.
DR   PANTHER; PTHR34384; PTHR34384; 1.
DR   Pfam; PF06276; FhuF; 1.
DR   Pfam; PF04183; IucA_IucC; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Nucleotide-binding; Plasmid; Transferase.
FT   CHAIN           1..575
FT                   /note="N(2)-citryl-N(6)-acetyl-N(6)-hydroxylysine synthase"
FT                   /id="PRO_0000084274"
SQ   SEQUENCE   575 AA;  65570 MW;  5E9883A747F415C4 CRC64;
     MILPSEKSAT DVAAQCFLNA LIRETKDWQL AEYPPDELII PLDEQKSLHF RVAYFSPTQH
     HRFAFPAHLV TASGSYPVDF TTLSRLIIDK LRHQLFLPVP LCETFHQRVL ESYAHTQQTI
     DARHDWAILR EKALNFGEAE QALLTGHAFH PAPKSHEPFN RQEAERYLPD MAPHFPLRWF
     SVDKTQIAGE SLHLNLQQRL TRFAAENAPQ LLNELSDNQW LFPLRPWQGE YLFQQVWCQA
     LFAKGLIRDL GEAGTSWLPT TSSRSLYCAT SRDMIKFSLS VRLTNSVRTL SVKEVERGMR
     LARLAQTDGW QMLQARFPTF RVMQEDDWTG LRDLNGNIMQ ESLFSPAWKT LLLEQPQSQT
     NVLVSLTQAG PHGGDSLLVS AVKRLSDRLG ITVQQAAHAW VDAYCQQVLK PLFTAEADYG
     LVLLAHQQNI LVQMLGDLPV GFIYRDCQGS AFMPHATEWL DTIDEAQAEN IFTREQLLRY
     FPYYLLVNST FAVTAALGAA GLDSEANLMA RVRTLLAEVR DQVTHKTCLN YVLESPYWNV
     KGNFFCYLND HNENTIVDPS VIYFDFANPL QAQEV