C5172_DICDI
ID C5172_DICDI Reviewed; 510 AA.
AC Q1ZXF3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable cytochrome P450 517A2;
DE EC=1.14.-.-;
GN Name=cyp517A2; ORFNames=DDB_G0284647;
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; AAFI02000070; EAS66858.1; -; Genomic_DNA.
DR RefSeq; XP_001134541.1; XM_001134541.1.
DR AlphaFoldDB; Q1ZXF3; -.
DR SMR; Q1ZXF3; -.
DR STRING; 44689.DDB0232998; -.
DR PaxDb; Q1ZXF3; -.
DR EnsemblProtists; EAS66858; EAS66858; DDB_G0284647.
DR GeneID; 8624702; -.
DR KEGG; ddi:DDB_G0284647; -.
DR dictyBase; DDB_G0284647; cyp517A2.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; Q1ZXF3; -.
DR PhylomeDB; Q1ZXF3; -.
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:Q1ZXF3; -.
DR Proteomes; UP000002195; Chromosome 4.
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; 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..510
FT /note="Probable cytochrome P450 517A2"
FT /id="PRO_0000318828"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 450
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 510 AA; 59381 MW; D323D74999A8C590 CRC64;
MRILIIIILI IIVFLVKDTI KKNKKVNSKS PCGPFAFPIL GNIIQYFFYQ ILNIKEHSMI
ERYSRKYDGI TRIWFGDIFI LYVSNYEIVK CFQKEENFFD RPSTFVPTWR YMSSNGGGIM
SSNDEKWKRA KTTFLKSLKI HGKKYLIEKK SIEFVNSIEK FSNSNQVFYP KQYSQGFTSS
IFFKYMFNED ISIDNKFLKE IGTAVGMVFT KNSHLTVFDC FGILSPFYDL FFKFRLRPIE
ILKKTIDKQL TNHLNSMDSK MGDHQSRDIM DDLLIEYGSL NEISNQDRIQ INQICFDVMS
TDIGTVATTI DWVLLQLCNR QDLQEIICNE IQDTIKIKRN NVINDGGGGA DTDNLFINLC
DKQSIPYLIA FIKETMRVFS NGWSLPKTSK HDQICANYFI PKGSILFINY FSIHLNEEFF
KNPREFNPAR YLDDSIPIPD LHFGIGQRGC PGRFVAMDQV FLCIANTLLK YKIKSIDGKK
IDDTIQFSVY LKPKDFGILL EKRNKLFVND
