ID A0A165QSS1_EXIGL Unreviewed; 502 AA.
AC A0A165QSS1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KZW04019.1};
GN ORFNames=EXIGLDRAFT_827954 {ECO:0000313|EMBL:KZW04019.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW04019.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW04019.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW04019.1,
RC ECO:0000313|Proteomes:UP000077266};
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}.
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DR EMBL; KV425882; KZW04019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QSS1; -.
DR STRING; 1314781.A0A165QSS1; -.
DR InParanoid; A0A165QSS1; -.
DR OrthoDB; 2289306at2759; -.
DR Proteomes; UP000077266; 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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11040; CYP7_CYP8-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24304:SF2; 24-HYDROXYCHOLESTEROL 7-ALPHA-HYDROXYLASE; 1.
DR PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
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 Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT BINDING 444
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 502 AA; 56161 MW; 210767D1E9B3E9B2 CRC64;
MLEAIPAART AAVAVGIAGA GTLVLCASLR YLRPLLARKN EPPTLSYWIP WLGHALWYMR
DARGLVDAAH EIFGSYSPFA VVLGGQKIYI VSDPPDVKAV YRAAKSLNFE PITAELVGGP
FGMGAAAAKL REAPPGEPNL ITIAHPFFRD ELTSRPRVQI ISERYLTALE GVMSGFARLF
KEADTQTVEV PMWRWCREVV FTASTNGIFG PMLIKQHPEL FDVYNAFDEE FYKLVFQFPD
SHTVDVRKHR AELLDMLVEF YSDMKTVEET AGDVISKWQQ QMIARSGMNP REMAAGALSL
FWGFNTNSLK TSFWMILFIC STPKLAARLR SEFAPAFVTQ SSLPNTDYLT KECPLLDATF
RETLRLATAP SSMRLVEEDT EIGGYTFYKG NRVLLPSMHL HRAKHFWGED ADSFRPERIL
EIGDKVDIVQ SGYLRPFGGG TSYCPGRIFS RSEIMAFVTL VLHRYDLELL GPVPVPNTGP
PTLGVLDPPM PCDLGLKLTR RY
//
