ID   C522A_DICDI             Reviewed;         489 AA.
AC   Q1ZXG3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable cytochrome P450 522A1;
DE            EC=1.14.-.-;
GN   Name=cyp522A1; ORFNames=DDB_G0282769;
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}.
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DR   EMBL; AAFI02000047; EAS66867.1; -; Genomic_DNA.
DR   RefSeq; XP_001134550.1; XM_001134550.1.
DR   AlphaFoldDB; Q1ZXG3; -.
DR   SMR; Q1ZXG3; -.
DR   STRING; 44689.DDB0233031; -.
DR   PaxDb; Q1ZXG3; -.
DR   EnsemblProtists; EAS66867; EAS66867; DDB_G0282769.
DR   GeneID; 8623617; -.
DR   KEGG; ddi:DDB_G0282769; -.
DR   dictyBase; DDB_G0282769; cyp522A1.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_558281_0_0_1; -.
DR   InParanoid; Q1ZXG3; -.
DR   PhylomeDB; Q1ZXG3; -.
DR   Reactome; R-DDI-211935; Fatty acids.
DR   Reactome; R-DDI-211958; Miscellaneous substrates.
DR   Reactome; R-DDI-211981; Xenobiotics.
DR   Reactome; R-DDI-211999; CYP2E1 reactions.
DR   Reactome; R-DDI-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
DR   Reactome; R-DDI-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
DR   Reactome; R-DDI-5423646; Aflatoxin activation and detoxification.
DR   Reactome; R-DDI-9027307; Biosynthesis of maresin-like SPMs.
DR   Reactome; R-DDI-9749641; Aspirin ADME.
DR   Reactome; R-DDI-9753281; Paracetamol ADME.
DR   PRO; PR:Q1ZXG3; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
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.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..489
FT                   /note="Probable cytochrome P450 522A1"
FT                   /id="PRO_0000318840"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         433
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   489 AA;  57076 MW;  CE3785988C580061 CRC64;
     MILTIVIIIL TVIFVNKYLL NNGGKNDLRK VQGPFNLPLL GALYAFDKER FHKSFDKFYD
     KYKDFYFIKF GQHDCIVLNS PKLIKQVVIE QSDSVFERFH TPSIKRYAQG KSILGCSPDE
     WKKLRSFIVI SFSKNKMGQQ VLDKIFHTQY LKFENHIKKL IKSNNNIVTL EPEFKRLTIS
     IIFNFQFGTD LEFTDPLIDS LLVCTEKIIA SCQKASDLMP IFEIFTSYKD IDGVVKEMYA
     LVKPFLEKYL KQHDRNNPKC ALDHMINCIL DQDEPKLITY EHLPHFLMDM FIGGTESTAR
     TMDWFTLMMT NRKEMQDRIR TELLDVGIRL PVLVDKQKYP LLNASIKEIH RLRPIQPIIA
     SRVVNDPIVL KHECSAKGES YTIPVGTLII PNAHSFNFDP QYHKDPLTFN PNRYIGDNPE
     ILHMTFDIGI RTCPFMSFAI DELFIIFSRL FQSFEFQPID NTPISEEAFT INSIRPKQWS
     CQVIERDHK