ID   NIT22_AJECA             Reviewed;         377 AA.
AC   B2KWH7;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Probable dehydratase NIT22 {ECO:0000303|PubMed:18404210};
DE            EC=1.-.-.- {ECO:0000305|PubMed:18404210};
DE   AltName: Full=Siderophore biosynthesis cluster protein NIT22 {ECO:0000303|PubMed:18404210};
GN   Name=NIT22 {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: Probable dehydratase; part of the gene cluster that mediates
CC       the 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   -!- INDUCTION: Expression is induced during iron deprivation
CC       (PubMed:18404210). {ECO:0000269|PubMed:18404210}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; EU253972; ACC64450.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2KWH7; -.
DR   SMR; B2KWH7; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR002539; MaoC-like_dom.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   SUPFAM; SSF54637; SSF54637; 2.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..377
FT                   /note="Probable dehydratase NIT22"
FT                   /id="PRO_0000444418"
FT   DOMAIN          233..332
FT                   /note="MaoC-like"
FT                   /evidence="ECO:0000255"
FT   REGION          220..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         24..32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         51..52
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         83..85
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         191..195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         224..226
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
SQ   SEQUENCE   377 AA;  41885 MW;  7678E41EEB5522E2 CRC64;
     MACPCGARVL VEILTGLLSL KNQSPSTPPE SEGEFTRNYI LGPKYIIKAI EIFSTMPNTI
     PPFEYAPVKT TWLKRDVLLF AHSIGCKAGD ELHFLYELHP KFQVFPTYPI VLTFKHADID
     IVDFLARNAA RTLPPGCPVL DWSVAVDGRR RMEFLCPLPP SSEGKTWDIH TKVLGVFDKG
     AGKGTVMEME HVLKQRESGQ VYTRAWESVF FKGTGGWGGE RGPKMNEHVP STPPRRPDAV
     SSFQSNAESA HLYRLNGDYN PLHATPEPGK SLGYGGTIMH GLFSWNITAR AVLSQFGGSE
     GRRLRDFEAM FSSPVKPGDK LDILMWDMGL CKRATSAVRN DESLQEVRFM VKVGDRVVLS
     NGKALLKCED EGVEVKL