ID   IUCA_VIBMI              Reviewed;         598 AA.
AC   Q76BS7;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 47.
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   Vibrio mimicus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=674;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=7PT;
RX   PubMed=15215626; DOI=10.1111/j.1348-0421.2004.tb03528.x;
RA   Moon Y.H., Tanabe T., Funahashi T., Shiuchi K., Nakao H., Yamamoto S.;
RT   "Identification and characterization of two contiguous operons required for
RT   aerobactin transport and biosynthesis in Vibrio mimicus.";
RL   Microbiol. Immunol. 48:389-398(2004).
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:15215626}.
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         Evidence={ECO:0000269|PubMed:15215626};
CC   -!- PATHWAY: Siderophore biosynthesis; aerobactin biosynthesis.
CC   -!- SIMILARITY: Belongs to the IucA/IucC family. {ECO:0000305}.
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DR   EMBL; AB110784; BAD02217.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q76BS7; -.
DR   SMR; Q76BS7; -.
DR   STRING; 675806.VII_002735; -.
DR   eggNOG; COG4264; Bacteria.
DR   UniPathway; UPA00014; -.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProt.
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; IEA:UniProtKB-UniPathway.
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; Transferase.
FT   CHAIN           1..598
FT                   /note="N(2)-citryl-N(6)-acetyl-N(6)-hydroxylysine synthase"
FT                   /id="PRO_0000418722"
SQ   SEQUENCE   598 AA;  67795 MW;  E7A2F38E4116B79A CRC64;
     MHRNNERINL EKSNDWANTN EPSIACFLNS LARESQSVQL LWGEDGKRVY RLPLANSDSI
     NIPLSYFSSL GSHEYCLPAL LHTQDSIKTL SVEQLIEHIV NEPALVGIVS EAKKAIFTKR
     VLESHRNTEQ AIEHSPYQEQ LFTEQLDFKT AEQGLLIGHS FHPAPKSREQ FSLSDAKLYS
     PELGGQFKLF WLSVEQSLLT SGSSADIHFN QRFEALVAHD PKLVEALQNA QQQGHELLPV
     HPWQWHVMVE NPSIKGYIAT KQIQNLGQLG ATWYPTSSTR SLYAPGLPYM LKFSLSVKLT
     NSIRNLSLKE CDSWNDLNDL FQHPQLAQQL GNGRGFQLMQ EPAYIGLKDL NGKIIDESLV
     AFRDNPLMNN PAEEAVVLAT LTQQNPYGGS SLVAARIEHY ATQQHLSLHQ AASLWFDAYC
     RHAVVPLFHL QANFGIVFLA HQQNIVMQLE QGFPVGMYYR DCQGTGYTDL AFKLFGEQLG
     DRKEALENYW NQDKVRRYFA YYLIINSTFN LISAICANLD VEESELIEIL YHNLNALLQS
     GVKDDLCLRY VLTSEALCCK GNFFCYLQNF NENSIPDPAV IYFDLPNPLA RVEEIAHV