ID U5NH23_9GENT Unreviewed; 518 AA. AC U5NH23; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 22-FEB-2023, entry version 20. DE SubName: Full=Secologanin synthase-like protein {ECO:0000313|EMBL:AGX93045.1}; DE Flags: Fragment; OS Cinchona calisaya. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Gentianales; Rubiaceae; Cinchonoideae; Cinchoneae; OC Cinchona. OX NCBI_TaxID=153742 {ECO:0000313|EMBL:AGX93045.1}; RN [1] {ECO:0000313|EMBL:AGX93045.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24103035; DOI=10.1111/tpj.12330; RA Salim V., Yu F., Altarejos J., De Luca V.; RT "Virus-induced gene silencing identifies Catharanthus roseus 7-deoxyloganic RT acid-7-hydroxylase, a step in iridoid and monoterpene indole alkaloid RT biosynthesis."; RL Plant J. 76:754-765(2013). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC {ECO:0000256|RuleBase:RU000461}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KF415098; AGX93045.1; -; mRNA. DR AlphaFoldDB; U5NH23; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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; IEA:UniProtKB-KW. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24282; CYTOCHROME P450 FAMILY MEMBER; 1. DR PANTHER; PTHR24282:SF255; CYTOCHROME P450, FAMILY 72, SUBFAMILY A, POLYPEPTIDE 9; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000461}; KW Monooxygenase {ECO:0000256|RuleBase:RU000461}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6..29 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AGX93045.1" SQ SEQUENCE 518 AA; 59588 MW; F7F908B12C3C7173 CRC64; MDIIHQAIAA TCIVALFAWA WRVLNWAWFT PKRIEKRLRQ QGFRGNPYRF LVGDAKESSM MLQKAMSKPI PFNNDIAPRI MPHLDKTIKT YGENSFTWDG TIPRIHILRP ELIREILTHS RKFQKHFAVQ NPLIELLLTG VGAYEGDKWS THRRIISPAL TLEKLKDMLS AFAVCYDGLL TKWEEIATED GSCEVDVFPT FDVLTSDVIS KVAFHSTYEE GLKIFLLLKE LMDHTIAAVR EFYIPGWSYL PTKRNRRMKN IDSDVRGMIR NIINKRLKAM KSGEPSEDDL LGVLLESNFK EIQKQGNKKN VGMTIDDVIE ECKLFYFAGQ ETTGVLLTWT MIMLSKHPEW QDRAREEVLH AFGKNTPEFD KLNHLKYVSM ILYEVLRLYP PVFDLNKVVY EDTKLGTYTI PAGTQIELPS VMIHRDKTIW GEDAMEFNPM RFANGVAAAT KNQVAYIPFS WGPRVCLGQN FAILQAKLGL TMILQRFSFD VSPSYVHAPF TILSLQPQFG SHVIFRKL //