C519D_DICDI
ID C519D_DICDI Reviewed; 566 AA.
AC Q54EM5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable cytochrome P450 519D1;
DE EC=1.14.-.-;
GN Name=cyp519D1; ORFNames=DDB_G0291448;
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; AAFI02000177; EAL61708.1; -; Genomic_DNA.
DR RefSeq; XP_635215.1; XM_630123.1.
DR AlphaFoldDB; Q54EM5; -.
DR SMR; Q54EM5; -.
DR PaxDb; Q54EM5; -.
DR EnsemblProtists; EAL61708; EAL61708; DDB_G0291448.
DR GeneID; 8628162; -.
DR KEGG; ddi:DDB_G0291448; -.
DR dictyBase; DDB_G0291448; cyp519D1.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q54EM5; -.
DR OMA; STFMQWI; -.
DR PhylomeDB; Q54EM5; -.
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:Q54EM5; -.
DR Proteomes; UP000002195; Chromosome 6.
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; 2.
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..566
FT /note="Probable cytochrome P450 519D1"
FT /id="PRO_0000318835"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 471..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 510
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 566 AA; 65732 MW; BB86BD5733B7C558 CRC64;
MNVFVLTFFI CIIYLLFDLI KKNKKLKDEP PTPKLALPLI GHLYLLGDRP NRSFLELSKR
YGGIFKIWMG EYPTVVLTDP DHVNEVWCKQ FLNFTNRPHF NSLDQFSSGF RNLSFSDYPL
WSELRKLVSS SFTKSKVKGI SNLLETQTNY LINTMNNYSI NNKPFNPKKY IHKLTLNVVC
MIAFSKEIKN DEDVNEGDMA RLTKPKEMIL KHLGSSNFCD FVPLVRPLFY LKNKRFDQTL
KQVREYIKEI YDDHLLNLDL NSPPKDIMDL LIMSTNDSKE DIIIQTCIDF LIAGSDTVGV
TIEWFLVYIS NNPIIQEKCF NELFNAFSNS NNTDNNNNNS TITTAIGFGD EYSSKTPFLN
ACIKEVLRIK PVTSLGLPRI ANDDTFVNGY RIPKGTQIIE NIYGLSNSDQ LIDDPTTFNP
YRWLEYQKLK SFQNDLKQQQ QQQQQQQQQQ QQLQLQQEQQ EQEQQKINLE FNNNNNNNNN
NNNNNSNNKH KYYNDLDKIS IPFSTGRRGC VGVQLGEAEL YIVCANLVYN FKIESWDGKK
INELEDFGII IHPSSHNLKI TKRNNK
