ID A0A2K3D9M5_CHLRE Unreviewed; 483 AA.
AC A0A2K3D9M5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CHLRE_10g427500v5 {ECO:0000313|EMBL:PNW77224.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW77224.1, ECO:0000313|Proteomes:UP000006906};
RN [1] {ECO:0000313|EMBL:PNW77224.1, ECO:0000313|Proteomes:UP000006906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906};
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CM008971; PNW77224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3D9M5; -.
DR STRING; 3055.A0A2K3D9M5; -.
DR PaxDb; 3055-EDP06329; -.
DR EnsemblPlants; PNW77224; PNW77224; CHLRE_10g427500v5.
DR Gramene; PNW77224; PNW77224; CHLRE_10g427500v5.
DR InParanoid; A0A2K3D9M5; -.
DR OrthoDB; 758626at2759; -.
DR Proteomes; UP000006906; Chromosome 10.
DR ExpressionAtlas; A0A2K3D9M5; baseline.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR CDD; cd00302; cytochrome_P450; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 2.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR PANTHER; PTHR24286:SF194; CYTOCHROME P450 26A1; 1.
DR Pfam; PF00067; p450; 2.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000006906}.
FT BINDING 428
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:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 483 AA; 51879 MW; 652C2AC02DE9A2FE CRC64;
MGVPLYVLTQ PADLRGPYRD QGAEPDVPFS SFRRLMEVAP GRPYDVQADK AAHGPWRRMF
LSALGPAGLQ ALLPRAQAVM QAHLAQWEAA GTAAGGRSGG GCIPSLFRQV RLLSVDLAIE
VIAEVPLPPG VERIAFREQL LCFLDGLFGL PLALPGSSVA RALAAKEELV AALGPLVAAD
RQRMAKRWRA AGSSYAALVD TLTAASAAVG GSAAAEAAAG VQAAEPSAAA AARVTVRDAV
ISGFMALGFE SERAAAVSVL HAVVAGADTT RFALFNTLAL VAMSARVQEE IFAEQERVVA
EHGPELSARV LGSAAITPYL DAVVREAMRL LPATPGNMRR LTADLRVGAG RGGPASELVI
PKGSMVWRFV PLMHCLDPVL WDGDTSVDVP AHMDWRSNFE GAFRPERWLS EDTKPKYYYT
FGSDNHLCVG QNLAYMEVKL LLAMLLRKYR LQLHTPDMLA RASQMFPFVI PRRGTDRVLL
EPR
//
