ID J3K2W8_COCIM Unreviewed; 1051 AA.
AC J3K2W8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Fatty acid oxygenase {ECO:0000313|EMBL:EAS28473.3};
GN ORFNames=CIMG_09677 {ECO:0000313|EMBL:EAS28473.3};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS28473.3, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; GG704912; EAS28473.3; -; Genomic_DNA.
DR RefSeq; XP_001240056.2; XM_001240055.2.
DR AlphaFoldDB; J3K2W8; -.
DR GeneID; 4558937; -.
DR KEGG; cim:CIMG_09677; -.
DR VEuPathDB; FungiDB:CIMG_09677; -.
DR InParanoid; J3K2W8; -.
DR OMA; EFNMIYR; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd20612; CYP_LDS-like_C; 1.
DR CDD; cd09817; linoleate_diol_synthase_like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR034812; Ppo-like_N.
DR PANTHER; PTHR11903:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 2.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001261}.
FT BINDING 357
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 1051 AA; 117670 MW; EC105B7C635FB4CE CRC64;
MDARKSDRDT QSGLANVLSG TMADIFSQTG RIGSDIQVIR EGAETMAAGG IIDDRQYTIE
HIIQLAASLP NGSKLRDKLT DQFVTTLWNN LEHPPLSYLG DQFKYRSADG SNNNIMYPHL
GASGSHYARS VVPQRPKMTN LPDPELIFET LMKRNGPSKD HPTKISSMLF HFATIIIHDI
FRTDELDISR LKNSSYLDLG PLYGHDEEQQ KGVRQFKDGL LKNDAFAEER VLGQPPGVCA
LLVAFNRFHN YVVGELATIN ERGRFTMPVE GSPNYEKALL KRDNDLFQTG RLVTCGLYIN
VILNDYLRAI LNLNDNDKDS DWKLDPRLAV GIFDATGVPR GVGNQVSAEF NVIYRFHPAV
SNNDEAWANQ FFKDVFGNDK DPAKISVNEF RLGIWNWMRK LDKDPAKREF GGLKRQSNGM
FKDSDLVKLL QESTEAVAGS FGGRNVPAVM KVVEMLGIEQ GRQWGLATLN EFRAFFKLKR
HEKFLDVNSD PSIAETLESL YGHPDDIELY TGVHVEEAKK PFMPGSGLCP GFTVSTAILY
DAVALVRGDR FYTIDYSPES LTSFGFSVAN SSFDVAKGGV MYKLLMRAFP SWYRPNSVYA
LFPFTTPEKN REVFTKHGSV NQYSFDRPSL TMPPIPVSTW KGVVDVLNDQ ARFKVPWGPH
TFEMTKHDYM LSGDSKANAE QREFVSKCLF EPKKGLEEVR KFYEAVTLNF LRKHGRKAGN
TYQVDAVREI GNLVHANFAG HFFQIPLQSA SGGPDSFTEQ ELYDSLAHLF AYVFLDVDPA
KSFERSVVGA RDSARLGKVV SQAVAAVQAG GFFFFKHLEH AKPEILSEYG ARLVERLSRG
RKSVDEVTWT IIPTAAASVA TQAQGWAQMF DLYMSDKYYS HWKTIEKLSR SDAPEDFEKL
KRYALEGLRL ATPAYGVLRV AATNGTIQDG SRTVSYKPGD VIFTNFMTAG ADPSKFPDPE
AIKLDRPEED YIHHGWGPHA CLGRPFVTTA AASMLRVFGR LDNVRRAPGP PGEMKSKVEG
GVFKVFLTPD GGDWNAFPCT KRVLFDGFRD V
//
