ID A0A094EMK1_9PEZI Unreviewed; 1043 AA.
AC A0A094EMK1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=V499_07009 {ECO:0000313|EMBL:KFY72875.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY72875.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY72875.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY72875.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY72875.1}.
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DR EMBL; JPKB01001162; KFY72875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EMK1; -.
DR HOGENOM; CLU_292238_0_0_1; -.
DR Proteomes; UP000029295; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR24304:SF2; 24-HYDROXYCHOLESTEROL 7-ALPHA-HYDROXYLASE; 1.
DR PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 43..209
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT BINDING 982
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 1043 AA; 114770 MW; 2AE5ADD6EE38BE25 CRC64;
MTSQLDNSRA TLRLFLNNHP EIKYVSPTDP EFSSLKIIYN QSVSVAPMAI VRPQTANDVA
ALVYFCVGSS IQFTIRSGGN NIYGLSCVQD ALMIDLRDIN YIEVDQTKSS VTVGGGVIVS
NLLRELSKDG LVTPTGALGF LGIVGWSTYG GYGPIMSRYG LGVDNILAAK VVNAKGEVVV
ANKELLKGIR GAGGALGVIV ELTVKVYPLG QVLAGMIIFD SQDITSTYKN FNAGYQALLE
DGSVPLELGI YQFIMNAPHG RVFALALVWS SEDHDAGRAT IAKIAALGPV MMNTVEPKTI
ADHIDFIGTQ VPQRAYGTCQ TVSIRKLNED ATEILGRAFE KMPSSFGTSF GVHELRGLSA
APNSDSVFSS REPHFMLELI SLVAKEEEVN ESIEWATGLK NELLQMDPKN LLSGTYISVT
QPGDVPLSKI YGPGSNFEAL LGLKRRYDPQ NAFSLAVVSY SMAMFDDLVA EGYSLAQRDW
RLTIVVASLL PFALTYLITS LRAFLAANNK SDSRSAPIAP YAVPFVGNLI SFLYDNERAV
RNALSRHARD VPVRFRLANR KLTLISGTAN VLAMFRGSRY LDSTEIIIIT VDNAFGGAGA
GRESYALDDT GSRKEPLPGS RPLNMSDRIW YLQHKTVHTN LVGPPLVEIA ERFVQYMGEE
LDRAIPESET DWVDVPDFYG LIQSTMFAAS TNAIYGPHLI GLNPDINKDF WEYDHHIPTL
FKLVPRLFAP KAYAVRDRLL ASIKKWQAHA RANLDFNDPK LEGVVWEEFY GSKMMRDRAV
DYTGVKGMTD DVRPTFDIGL LWAANANIVP TVGWCLIDIL TRPALAATAR AEIAALSPGG
GIDMQALLAS PLLQSIYAEE LRLRNAIFIQ RTPIVDTFKI GPWKFPKGDL IIASSWQEAR
NRETWNQHGR DGEKHDVEEF WAERFLVYKD HPLSGPRLID PAKLKGGEEA EKAEGGEAVP
PKFAPEKVAG QFIPYGGGEN ICPGRFYAKQ EAMAGMALFL SKFEIELQLE PGRVLEPNKK
QFGFGVMGPK GEIKARMRRR KAE
//
