ID   SID4_AJECA              Reviewed;         589 AA.
AC   B2KWI3;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Acyl-CoA ligase SID4 {ECO:0000303|PubMed:18404210};
DE            EC=6.2.1.- {ECO:0000305|PubMed:18404210};
DE   AltName: Full=Siderophore biosynthesis cluster protein SID4 {ECO:0000303|PubMed:18404210};
GN   Name=SID4 {ECO:0000303|PubMed:18404210};
OS   Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=5037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=ATCC 26032 / G217B;
RX   PubMed=18404210; DOI=10.1371/journal.ppat.1000044;
RA   Hwang L.H., Mayfield J.A., Rine J., Sil A.;
RT   "Histoplasma requires SID1, a member of an iron-regulated siderophore gene
RT   cluster, for host colonization.";
RL   PLoS Pathog. 4:E1000044-E1000044(2008).
CC   -!- FUNCTION: Acyl-CoA ligase; part of the gene cluster that mediates the
CC       biosynthesis of hydroxamate-containing siderophores that play a
CC       critical role in virulence via intracellular iron acquisition during
CC       macrophage infection (PubMed:18404210). {ECO:0000269|PubMed:18404210}.
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000305|PubMed:18404210}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q4WR83}.
CC       Note=Targeted to peroxisomes via its PTS2-type peroxisomal targeting
CC       signal (By similarity). {ECO:0000250|UniProtKB:Q4WR83}.
CC   -!- INDUCTION: Expression is induced during iron deprivation
CC       (PubMed:18404210). {ECO:0000269|PubMed:18404210}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; EU253978; ACC64456.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2KWI3; -.
DR   SMR; B2KWI3; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Nucleotide-binding; Peroxisome.
FT   CHAIN           1..589
FT                   /note="Acyl-CoA ligase SID4"
FT                   /id="PRO_0000444398"
FT   MOTIF           12..20
FT                   /note="PTS2-type peroxisomal targeting signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WR83"
FT   BINDING         228..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         367..372
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         372
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         458
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         473
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         481..483
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         547
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         555..557
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         572
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ   SEQUENCE   589 AA;  65269 MW;  38C66CCD2644D48D CRC64;
     MATISNETPL WRLQQTLNHI LPQSVRKNEK HLAVVHGPTQ PALWEMTLGE LLEFQCLRYR
     DLEAVVVPWT AARWTYGQLE NESSHLARGL LAKGIQRGDR IGVMAGNCEE YVSLFFAAAR
     VGAILVVINN TYTDAELKYA LSHTACKLLF IVPRIGRHDL KNALEDLHSP DISKRLPNLN
     ETVMIQGSFK SFGTYKDVIL AGNVVPLSAV QRRQDTLSPF DVCNLQFTSG STGNPKASML
     THHNLINNSR FIGDRMDFTE YDILCCPPPL FHCFGLVLGL LACITHGAKV VYPAETFDPE
     AVLRAISDER CTALHGVPTM FEAILALSRP DSFDCSQLRT GIIAGAPVPR PLMKRLWNEL
     NMTEFTSSYG LTEASPTCFN AFTSDSIATR LTTVGKVLPH ASAKIINPET GETVKIGERG
     ELCMSGYQIH KGYWGNLEKT AEALIEDEDG TIWLRTGDEA VFNSDGYCTI TGRFKDIIIR
     GGENIYPLEI EERLTAHPAI SRAAVVGLPN KHYGEIVGAF LVLEPGHTCP PDDEIKNWTR
     QTLGRHKAPK HVFVFGLDPR LPLDMPQTGS GKIQKQVLRD LGKRLVGEE