OXR1_AJECA
ID OXR1_AJECA Reviewed; 463 AA.
AC B2KWH9;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Oxidoreductase OXR1 {ECO:0000303|PubMed:18404210};
DE EC=1.-.-.- {ECO:0000305|PubMed:18404210};
DE AltName: Full=Siderophore biosynthesis cluster protein OXR1 {ECO:0000303|PubMed:18404210};
GN Name=OXR1 {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).
RN [2]
RP INDUCTION.
RX PubMed=22117028; DOI=10.1128/ec.05274-11;
RA Hwang L.H., Seth E., Gilmore S.A., Sil A.;
RT "SRE1 regulates iron-dependent and -independent pathways in the fungal
RT pathogen Histoplasma capsulatum.";
RL Eukaryot. Cell 11:16-25(2012).
CC -!- FUNCTION: Oxidoreductase; 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 -!- COFACTOR:
CC Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470;
CC Evidence={ECO:0000250|UniProtKB:Q9BRQ8};
CC Note=Binds 6-hydroxy-FAD non-covalently.
CC {ECO:0000250|UniProtKB:Q9BRQ8};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000305|PubMed:18404210}.
CC -!- INDUCTION: Expression is induced during iron deprivation and is
CC regulated by the transcription factor SRE1 (PubMed:18404210,
CC PubMed:22117028). {ECO:0000269|PubMed:18404210,
CC ECO:0000269|PubMed:22117028}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; EU253974; ACC64452.1; -; Genomic_DNA.
DR AlphaFoldDB; B2KWH9; -.
DR SMR; B2KWH9; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..463
FT /note="Oxidoreductase OXR1"
FT /id="PRO_0000444411"
FT BINDING 59..63
FT /ligand="6-hydroxy-FAD"
FT /ligand_id="ChEBI:CHEBI:60470"
FT /evidence="ECO:0000255"
FT BINDING 154
FT /ligand="6-hydroxy-FAD"
FT /ligand_id="ChEBI:CHEBI:60470"
FT /evidence="ECO:0000255"
FT BINDING 366
FT /ligand="6-hydroxy-FAD"
FT /ligand_id="ChEBI:CHEBI:60470"
FT /evidence="ECO:0000255"
SQ SEQUENCE 463 AA; 50819 MW; 14D4A35B2A7AB725 CRC64;
MLSLFYQRIS TYIKLSASSL LSILPLYRPF QRRRLTMPSN EGSISSSSTT RPKDVLVVGG
SYSGLAAALN LLDLCQGRSC RFAGALDPEI SEPAEMRERV PVQITIVDER DGYFHLIGTP
LAFASEEYAL SAWRKFADIP ALQTPAIKFI QGSVTRVDCE RKISTIKEAG TNNEISQKYD
YLVASSGLRR TWPSAPQSLN KDKYLEEVGE HIAKIKMANG GVVVIGGGAV GIEMASELKE
MHPDLRVTLI HSRAKLLSSE PLPDEFRDRA LELLHETGVE TILGSRVIRT TQTELNGAAT
PSYTLSLTDG RTIKAGYVIN AISKYSPTTA YLPSSVLDKE GYVKVNSALN FTDEVPNAKY
HFAAGDLALW SGIKRAGRAM HHGHYVGMNI YQQLLNERFG TKPKFSEMAH APPSMAVAVG
KNTVAYGTEQ GVVSGEEIAK IFFEDDLGFG ICWRYLKLGE APK