ID A0A163JNT1_ABSGL Unreviewed; 518 AA.
AC A0A163JNT1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=sterol 22-desaturase {ECO:0000256|ARBA:ARBA00039038};
DE EC=1.14.19.41 {ECO:0000256|ARBA:ARBA00039038};
GN Name=ABSGL_07982.1 scaffold 9429 {ECO:0000313|EMBL:SAM02211.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM02211.1};
RN [1] {ECO:0000313|EMBL:SAM02211.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM02211.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; LT553750; SAM02211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163JNT1; -.
DR STRING; 4829.A0A163JNT1; -.
DR InParanoid; A0A163JNT1; -.
DR OMA; WMQAIVE; -.
DR OrthoDB; 5393233at2759; -.
DR Proteomes; UP000078561; 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:UP000078561}.
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 518 AA; 58911 MW; 8B8F0C3843144A8E CRC64;
MASSSLFDPR MIESTKNTIA AFIKTMFSQK PTVSTTAVVC SAVVGLFAYE QYVYLNKKKG
LPGPKLKIPV IGAFMDSLYP TFEGYMNKWK SGELSCVGVF DRFVVIASTC DLSRKILNSP
VYAEPAVVAS MKHILCDDNW VFLSGKSHVD YRRGLNVLFT RKALGMYIPI QESVYQKHFD
KWLSFGGEKQ QFQWHFRELN MESSLRVFLG FHMSDKVAET ISEEYFNITA ALELVNFPIP
LPGTKVYKAI QSRKYIVHHF IESIKDARVR MDNGGEVKSM MDAWISAMKE NELECEREGK
PAPRKFDDRE VALTILTFLF ASQDATSSAM TWAFQLLADH PDVLEKVRQE QIKVRKGNLD
TELSLELMEE SVYLRQVVKE ILRLRPPVLM VPYQTVREWP LTSTYTVPKG AMLIPTTYPA
LHDPVAYPNP DSFDPDRWGP SGHAEKYPKN FMVFGNGSHH CLGKEYAVMH LMATMAQAAL
QLDWTHYRTD KSDDISIFAT IYPQDGCIMS FHPRAATA
//
