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Database: UniProt
Entry: A0A179UVV7_BLAGS
LinkDB: A0A179UVV7_BLAGS
Original site: A0A179UVV7_BLAGS 
ID   A0A179UVV7_BLAGS        Unreviewed;       624 AA.
AC   A0A179UVV7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Dioxygenase {ECO:0000313|EMBL:OAT12236.1, ECO:0000313|EMBL:OAT12237.1};
GN   ORFNames=BDBG_07612 {ECO:0000313|EMBL:OAT12236.1};
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT12236.1, ECO:0000313|Proteomes:UP000002038};
RN   [1] {ECO:0000313|EMBL:OAT12236.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SLH14081 {ECO:0000313|EMBL:OAT12236.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center.;
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Klein B., Goldman B., Young S.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Heiman D.I.,
RA   Hepburn T.A., Saif S., Shea T.D., Shenoy N., Sykes S., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Blastomyces dermatitidis strain SLH14081.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006787}.
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DR   EMBL; GG657466; OAT12236.1; -; Genomic_DNA.
DR   EMBL; GG657466; OAT12237.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A179UVV7; -.
DR   STRING; 559298.A0A179UVV7; -.
DR   VEuPathDB; FungiDB:BDBG_07612; -.
DR   OrthoDB; 294919at2759; -.
DR   Proteomes; UP000002038; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR   InterPro; IPR004294; Carotenoid_Oase.
DR   PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR   PANTHER; PTHR10543:SF24; CAROTENOID ISOMEROOXYGENASE; 1.
DR   Pfam; PF03055; RPE65; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000313|EMBL:OAT12236.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR604294-1};
KW   Oxidoreductase {ECO:0000313|EMBL:OAT12236.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002038}.
FT   REGION          20..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         245
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         295
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         369
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         609
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   624 AA;  68334 MW;  A3B0684C4A627218 CRC64;
     MTSSLRQVVS SRKRLTQITT AHTMGAVDTS TKSSNDWPNH QGFNSTYEER TPVELKVTGD
     IPAWAAGVLY RTGTGRSEIE TDQRQTFKVA HWFDGLAVVH RFQILPPDAT HPSVRVFYNS
     RSCCDGLIER IRKTGKGNEM SFAAKYDPCT SYFQKAMSLF RPAPPKTPGA DQQSMSITLS
     VNFPGLSSST TTQKTSGHAS GIHTLTNKTD AAVFQTLDPE TLEPIGLASQ QVLHPALKGP
     ISAAHAKSDP ATGDVYNFNL ELGKCPIYRI FHVSAATGKT SVLATLTNAR AAYLHSLFLT
     EHYVILCVWN SYFTAGGLAI LWHKNIVDAI ADYDPSKKST WYVIDRRPTD QGGRGLVATY
     KSDPFFCFHT VNAYEEPSPD GSGDIDIVAD LTTYNNLDII KRFYLSNIVS TSPNAAKYAA
     GIDPASRAIY KRFRLPSVPV PSPSSSTPTP SKASKPKRAI LDFKNEAANT PELPTLNPHY
     VTRRHRYVYG VTDSGKSSFL DGLVKVDTET KQTIHWKEWG QNPGEPIFVQ RRIIPRQEGE
     SGSENDSEDA VGEVEKEVDA DVFDEDDGVL LSVVLDGLKG KSYLLVLDAK NLKEVGRAEV
     AGPIGFGFHG THVSAMSGGR GLDY
//
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