ID CPXL_PSESP Reviewed; 428 AA. AC P33006; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 111. DE RecName: Full=Cytochrome P450-terp; DE Short=Cytochrome P450terp; DE EC=1.14.-.-; DE AltName: Full=Cytochrome P450 108; GN Name=cyp108; Synonyms=terPC; OS Pseudomonas sp. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=306; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=1629218; DOI=10.1016/s0021-9258(19)49697-x; RA Peterson J.A., Lu J.-Y., Geisselsoder J., Graham-Lorence S., Carmona C., RA Witney F., Lorence M.C.; RT "Cytochrome P-450terp. Isolation and purification of the protein and RT cloning and sequencing of its operon."; RL J. Biol. Chem. 267:14193-14203(1992). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=8120894; DOI=10.1016/0022-2836(94)90019-1; RA Hasemann C.A., Ravichandran K.G., Peterson J.A., Deisenhifer J.; RT "Crystal structure and refinement of cytochrome P450terp at 2.3-A RT resolution."; RL J. Mol. Biol. 236:1169-1185(1994). CC -!- FUNCTION: Catalyzes the hydroxylation of alpha-terpineol. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}. 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; M91440; AAA25996.1; -; Genomic_DNA. DR PIR; A42971; A42971. DR PDB; 1CPT; X-ray; 2.30 A; A=1-428. DR PDB; 8EUH; X-ray; 2.00 A; A=1-428. DR PDB; 8EUK; X-ray; 1.98 A; A=1-428. DR PDB; 8EUL; X-ray; 2.24 A; A=1-428. DR AlphaFoldDB; P33006; -. DR SMR; P33006; -. DR KEGG; ag:AAA25996; -. DR EvolutionaryTrace; P33006; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:InterPro. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR CDD; cd11033; CYP142-like; 1. DR FunFam; 1.10.630.10:FF:000018; Cytochrome P450 monooxygenase; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR002397; Cyt_P450_B. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR036396; Cyt_P450_sf. DR PANTHER; PTHR46696:SF1; CYTOCHROME P450 YJIB-RELATED; 1. DR PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00359; BP450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. DR PDBsum; 1CPT; -. DR PDBsum; 8EUH; -. DR PDBsum; 8EUK; -. DR PDBsum; 8EUL; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Heme; Iron; KW Metal-binding; Monooxygenase; Oxidoreductase. FT CHAIN 1..428 FT /note="Cytochrome P450-terp" FT /id="PRO_0000052222" FT BINDING 377 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 HELIX 9..16 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 19..22 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 24..37 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 39..43 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 57..64 FT /evidence="ECO:0007829|PDB:8EUK" FT TURN 67..69 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 70..75 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 82..90 FT /evidence="ECO:0007829|PDB:8EUK" FT TURN 91..94 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 109..115 FT /evidence="ECO:0007829|PDB:8EUK" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 123..126 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 130..145 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 147..152 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 154..158 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 161..170 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 174..176 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 177..181 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 182..187 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 205..232 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 238..243 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 246..251 FT /evidence="ECO:0007829|PDB:1CPT" FT HELIX 254..285 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 287..295 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 297..299 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 300..311 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 317..323 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 325..327 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 330..332 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 337..340 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 342..345 FT /evidence="ECO:0007829|PDB:8EUK" FT TURN 349..351 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 380..394 FT /evidence="ECO:0007829|PDB:8EUK" FT HELIX 395..397 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 398..405 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 408..410 FT /evidence="ECO:0007829|PDB:8EUL" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 417..420 FT /evidence="ECO:0007829|PDB:8EUK" FT STRAND 422..427 FT /evidence="ECO:0007829|PDB:8EUK" SQ SEQUENCE 428 AA; 47922 MW; 29B772460CC4E93F CRC64; MDARATIPEH IARTVILPQG YADDEVIYPA FKWLRDEQPL AMAHIEGYDP MWIATKHADV MQIGKQPGLF SNAEGSEILY DQNNEAFMRS ISGGCPHVID SLTSMDPPTH TAYRGLTLNW FQPASIRKLE ENIRRIAQAS VQRLLDFDGE CDFMTDCALY YPLHVVMTAL GVPEDDEPLM LKLTQDFFGV HEPDEQAVAA PRQSADEAAR RFHETIATFY DYFNGFTVDR RSCPKDDVMS LLANSKLDGN YIDDKYINAY YVAIATAGHD TTSSSSGGAI IGLSRNPEQL ALAKSDPALI PRLVDEAVRW TAPVKSFMRT ALADTEVRGQ NIKRGDRIML SYPSANRDEE VFSNPDEFDI TRFPNRHLGF GWGAHMCLGQ HLAKLEMKIF FEELLPKLKS VELSGPPRLV ATNFVGGPKN VPIRFTKA //