C521A_DICDI
ID C521A_DICDI Reviewed; 491 AA.
AC Q1ZXA1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Cytochrome P450 monooxygenase 521A1 {ECO:0000303|PubMed:31063135};
DE EC=1.14.-.- {ECO:0000269|PubMed:31063135};
DE AltName: Full=Discodiene biosynthesis cluster protein cyp521A1 {ECO:0000303|PubMed:31063135};
GN Name=cyp521A1; ORFNames=DDB_G0293738;
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).
RN [2]
RP INDUCTION, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=31063135; DOI=10.7554/elife.44352;
RA Chen X., Luck K., Rabe P., Dinh C.Q., Shaulsky G., Nelson D.R.,
RA Gershenzon J., Dickschat J.S., Koellner T.G., Chen F.;
RT "A terpene synthase-cytochrome P450 cluster in Dictyostelium discoideum
RT produces a novel trisnorsesquiterpene.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the trisnorsesquiterpene discodiene which
CC has a function during later stages of multicellular development, during
CC the transition from fingers to Mexican hats (PubMed:31063135). The
CC terpene synthase tps8 converts its substrate farnesyl diphosphate (FDP)
CC into the bicyclic sesquiterpene alcohol discoidol (PubMed:31063135).
CC The cytochrome P450 monooxygenase cyp521A1 then catalyzes the oxidative
CC degradation of discoidol to form the trisnorsesquiterpene discodiene
CC (PubMed:31063135). {ECO:0000269|PubMed:31063135}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:31063135}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Expression is almost undetectable in vegetatively growing
CC cells (PubMed:31063135). Small amounts of transcripts accumulate
CC between 4-8 hrs of development, continue to accumulate until they peak
CC at 16 hrs, and decline thereafter (PubMed:31063135).
CC {ECO:0000269|PubMed:31063135}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AAFI02000218; EAS66806.1; -; Genomic_DNA.
DR RefSeq; XP_001134489.1; XM_001134489.1.
DR AlphaFoldDB; Q1ZXA1; -.
DR SMR; Q1ZXA1; -.
DR STRING; 44689.DDB0233030; -.
DR PaxDb; Q1ZXA1; -.
DR PRIDE; Q1ZXA1; -.
DR EnsemblProtists; EAS66806; EAS66806; DDB_G0293738.
DR GeneID; 8629378; -.
DR KEGG; ddi:DDB_G0293738; -.
DR dictyBase; DDB_G0293738; cyp521A1.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q1ZXA1; -.
DR OMA; CPGEYLA; -.
DR PhylomeDB; Q1ZXA1; -.
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:Q1ZXA1; -.
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; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..491
FT /note="Cytochrome P450 monooxygenase 521A1"
FT /id="PRO_0000318839"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 438
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|UniProtKB:P04798"
SQ SEQUENCE 491 AA; 56808 MW; 81C2BB88E24DD32C CRC64;
MILLTLLYLI IFYIIIDFIK KNYKTKNQLP SPLGIALPII GHLHLLRTDP YKTLAKASKK
TEHGILKCWN GEHLMVVVDN PSIIKQMYVN TNNFTDRPQT KVFEIISRNY KNSGFANGEK
WKHLRGLYAP SFTKIKSRPH ENIILKYVNF EIKSLKNHAI TNSIYNPFLI ENINSFGTKV
ITEIIFGREF SENEVYSLIG PMNKLFGILD TPFPSESISF LKPFYRRSYK ECDKQCEELF
KLVEKVYDDH LLNLDKDNPK DVMDVMIVET DFKEKDHVIC ICCDLLMGTK DTFNTIVLWF
FVLMINYQDV QLKGYQEIIK VLECTGRDHV TIEDIDKLPY IDGIIKEISR IHPAGPLSVP
RTAINDIMIN GYFIPKGCHV FQNTYGAVYN YMKESDEPCK MKPERWIENE KLRKDGKLDP
TNDLALISLP FSSGIRNCPG VGFAEYELFL LFSNIILNFH LSSPNNLKLN ESGHFGLTMK
PFPFLVDLKL R
