CPXL_PSESP
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 03-AUG-2022, entry version 99.
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; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC 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}.
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DR EMBL; M91440; AAA25996.1; -; Genomic_DNA.
DR PIR; A42971; A42971.
DR PDB; 1CPT; X-ray; 2.30 A; A=1-428.
DR PDBsum; 1CPT; -.
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: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; -; 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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
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:1CPT"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:1CPT"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1CPT"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1CPT"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:1CPT"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 208..230
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 254..285
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:1CPT"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 380..394
FT /evidence="ECO:0007829|PDB:1CPT"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 398..405
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:1CPT"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:1CPT"
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
