ID A0A165DJQ6_9BASI Unreviewed; 517 AA.
AC A0A165DJQ6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=sterol 22-desaturase {ECO:0000256|ARBA:ARBA00039038};
DE EC=1.14.19.41 {ECO:0000256|ARBA:ARBA00039038};
GN ORFNames=CALCODRAFT_501628 {ECO:0000313|EMBL:KZT52959.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT52959.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT52959.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT52959.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KV424050; KZT52959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165DJQ6; -.
DR STRING; 1353952.A0A165DJQ6; -.
DR InParanoid; A0A165DJQ6; -.
DR OrthoDB; 5393233at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
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:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11082; CYP61_CYP710; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24286:SF228; C-22 STEROL DESATURASE ERG5; 1.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT BINDING 461
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 517 AA; 58691 MW; B26CBEA25833E8F9 CRC64;
MASSHSAPVP TAESSPLAFF FDQFHAQLPF QLTFPPALPT LNVWTSLAIV VLSLLVLEQT
VWRVKRKFLP GDKWTIPVIG QFVNSLHPSL ENYQKQWARG PLSATSVFNM FIVIASANEF
VRKIFNSSGT YTEPMLVAAA RPILEHDNWV FLNGKVHIDY RRMLNQFFTR KSLSMYLATQ
DIIARDHFKM WLADSTDEAK EVMIPMRFFN MATSLRVFCG SYVPDDVVRL ISDKYFLITK
AMELVNFPLH LPGTKVYNAI QARKVAMKYL LEAATASKAN MRAGGEPNCL MDEWCKVMFA
QDREYSDKEM AQVVLSFLFA SQDAMTSGLI YAFQHLADHP EVLAKVREEQ ERIRGGDVDR
AITLEELDSC TYLRATVKES LRLKPPVLMV PYKVTEAFPI SPTYTVPAGS MVIPSLYPSL
HDPEVYPEPK KFLPERWLDP KGTAEQNPKN YLVFGAGAHR CIGYEYALMH IAMVVGTASV
LMDWQHVATP QSEKVQIIAT IFPKDGCLLR WSPRQRK
//
