ID   C524A_DICDI             Reviewed;         532 AA.
AC   Q55EK2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable cytochrome P450 524A1;
DE            EC=1.14.-.-;
GN   Name=cyp524A1; ORFNames=DDB_G0269016;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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; AAFI02000004; EAL73097.1; -; Genomic_DNA.
DR   RefSeq; XP_647018.1; XM_641926.1.
DR   AlphaFoldDB; Q55EK2; -.
DR   SMR; Q55EK2; -.
DR   STRING; 44689.DDB0233032; -.
DR   PaxDb; Q55EK2; -.
DR   EnsemblProtists; EAL73097; EAL73097; DDB_G0269016.
DR   GeneID; 8616711; -.
DR   KEGG; ddi:DDB_G0269016; -.
DR   dictyBase; DDB_G0269016; cyp524A1.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_023517_1_0_1; -.
DR   InParanoid; Q55EK2; -.
DR   OMA; MVIPSFY; -.
DR   PhylomeDB; Q55EK2; -.
DR   PRO; PR:Q55EK2; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0016021; C:integral component of 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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..532
FT                   /note="Probable cytochrome P450 524A1"
FT                   /id="PRO_0000318841"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         478
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:0000250"
SQ   SEQUENCE   532 AA;  59871 MW;  5E4D7F8641CB754A CRC64;
     MKTPTKYFII FILLAALAVF VSEATSKVGQ QTTTTTQQVK CSGLQCTLNK LIVAVGKFTI
     KQILVGIVIV LATIALHQQY VITQKKGSLP GPSFVPPFFG MLFQLIFTPF SFYEKQEKYG
     PISWTSIMNK FVLFVTDAEI NRQVFKEENA KLYLSLGAKK ILTEKAIPFI EGAPHRQLRK
     QLLPLFTIRA LSSYLPIQES IVDEHIAMWI KNGKADINAR NNCRDLNMAI STGVFVGNNT
     PESVRDDIAK NFFVMNEGFL CLPIDLPGTT LRKAINARVR LVEIFTDIIA KSRKRMGDGE
     KPQSLIDLWV EHFLNCPEEE RDELSNDTII FTLLSFMFAS QDALTSSLVW TVQLMAEHPD
     ILAKVRAEQA SLRPNNEKLD LDTMRQATYT RMVVSEILRF RPPAVMVPHE NIEDIVIGDN
     VHVPKGTMIL PSIWSAHFQE GGYSDPYKFD PQRFDSVRKE DVTCAKNSLV FGAGPHFCIG
     KELAKNQIEV FLTKLAMSTE WTHNKTPGGD EIIFGPTIFP KDGCNITIKA RN