C519B_DICDI
ID C519B_DICDI Reviewed; 509 AA.
AC Q54Q53;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable cytochrome P450 519B1;
DE EC=1.14.-.-;
GN Name=cyp519B1; ORFNames=DDB_G0284089;
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; AAFI02000063; EAL65385.1; -; Genomic_DNA.
DR RefSeq; XP_638744.1; XM_633652.1.
DR AlphaFoldDB; Q54Q53; -.
DR SMR; Q54Q53; -.
DR STRING; 44689.DDB0233020; -.
DR PaxDb; Q54Q53; -.
DR EnsemblProtists; EAL65385; EAL65385; DDB_G0284089.
DR GeneID; 8624414; -.
DR KEGG; ddi:DDB_G0284089; -.
DR dictyBase; DDB_G0284089; cyp519B1.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q54Q53; -.
DR OMA; NTVHHDP; -.
DR PhylomeDB; Q54Q53; -.
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:Q54Q53; -.
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..509
FT /note="Probable cytochrome P450 519B1"
FT /id="PRO_0000318833"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 456
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 509 AA; 59026 MW; E5E3BF0DC24CC4B2 CRC64;
MNLINLILYF ILFWIVFDFI RKNRRISFND PPSPWALPII GHLHKLSLNP HRSLTELAKV
YGGVYSLHIG DSKTVVITDV SAFKDVTIKQ FKNFANRPQP KSIRVITNFK GLAFADYDQW
QKTRKLVSSA LTKTKIKTFN NLIEKQTENL IESMNEFSNK NELFHPRKYL TKYSLNIILS
MLFSKEIGKN ESINKGTMER LTIPFNEAFK KVGKVDDFLW FLSPFFYFSN KQYKKYIFDI
YYFMEEIYDQ HLLDLDYNEP KDLLDQLIIA SQGREKETVI LVGMDFLLAG SDTQKATQEW
FCLYLINNPD VQKKAYQELI SVVGKDCKFV TSNHIENCPY FISIIKEVFR IRSPGPLGLP
RISIDDTYLS NGMFIPKGTQ ILLNIFGMGN LLVSEPDQFK PERWINYKNQ QQQKQQQQQQ
QVNNKNSIDS SESSNLEFFD DLEKVSNPFS LGPRNCVGMA IAKSSIYSVC SNILLNFELS
SINNQIIDDN EVFGVSINPK EFSIKLTKR
