GenomeNet

Database: UniProt
Entry: D4ANT9_ARTBC
LinkDB: D4ANT9_ARTBC
Original site: D4ANT9_ARTBC 
ID   D4ANT9_ARTBC            Unreviewed;       485 AA.
AC   D4ANT9;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Cytochrome P450 oxidoreductase GliF {ECO:0000313|EMBL:EFE34950.1};
GN   ORFNames=ARB_05906 {ECO:0000313|EMBL:EFE34950.1};
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE34950.1, ECO:0000313|Proteomes:UP000008866};
RN   [1] {ECO:0000313|Proteomes:UP000008866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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}.
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:EFE34950.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABSU01000004; EFE34950.1; -; Genomic_DNA.
DR   RefSeq; XP_003015595.1; XM_003015549.1.
DR   AlphaFoldDB; D4ANT9; -.
DR   STRING; 663331.D4ANT9; -.
DR   GeneID; 9525876; -.
DR   KEGG; abe:ARB_05906; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_022195_0_2_1; -.
DR   OMA; QMIILPR; -.
DR   OrthoDB; 1351063at2759; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11041; CYP503A1-like; 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; PTHR46206; CYTOCHROME P450; 1.
DR   PANTHER; PTHR46206:SF6; CYTOCHROME P450 MONOOXYGENASE GLIF; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008866};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         430
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   485 AA;  54584 MW;  9715A4B848CBE431 CRC64;
     MAGLLEAYPT THLWLVVLLL LGVLWICLKG ATGTRKVPAT GFPVIKLKSN DMEPGIIEGS
     KLYPDQPYEI QVPAKQMIIL PRKYLDEIKR FPESQMSFKA LVKDAMAGEY TMIATHDHSL
     VTALRRDLTQ NIVHAHELLQ EEAISVVKTK LGFCGNGSHV FMLWKVLTIG IKLGCILKYT
     EDAFKAGMIL HMTPSIIHPL LNMFLPQLWA VRRHYATVKR LVTAYLLVRL LKPILEERIE
     KLKDPAYKPP RDMIQSFINI NPQKGMSLDF QATNQLMAAF TSMHTTSMNA CHALFHLAAA
     PEHVAPLREE IETVLAEEGG LTSKAAMQKL RKLDSFLRET QRLNPSSFVG MERKVLVTTK
     LSDGTVLPAG SILGFDSFQI NYDTQLWENP EKFDGFRFAR LRAADGNDHK YQATSIGLES
     LSFGLGTHAC PGRFFAINET KILLAHLIMN YDWAFPDGQG RPKNFTLISA LLINPESEVL
     CRRRQ
//
DBGET integrated database retrieval system