CP119_SULAC
ID CP119_SULAC Reviewed; 368 AA.
AC Q55080; Q4J756;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytochrome P450 119;
DE EC=1.14.-.-;
DE AltName: Full=Peroxidase;
DE EC=1.11.1.7;
GN Name=cyp119; OrderedLocusNames=Saci_2081;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8617361; DOI=10.1016/0014-5793(96)00322-5;
RA Wright R.L., Harris K., Solow B., White R.H., Kennelly R.H.;
RT "Cloning of a potential cytochrome P450 from the archaeon Sulfolobus
RT solfataricus.";
RL FEBS Lett. 384:235-239(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9813164; DOI=10.1006/bbrc.1998.9584;
RA McLean M.A., Maves S.A., Weiss K.E., Krepich S., Sligar S.G.;
RT "Characterization of a cytochrome P450 from the acidothermophilic archaea
RT Sulfolobus solfataricus.";
RL Biochem. Biophys. Res. Commun. 252:166-172(1998).
RN [4]
RP FUNCTION, HEME BINDING, REACTION STEREOCHEMISTRY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF THR-213 AND THR-214.
RX PubMed=10799487; DOI=10.1074/jbc.275.19.14112;
RA Koo L.S., Tschirret-Guth R.A., Straub W.E., Moenne-Loccoz P., Loehr T.M.,
RA Ortiz de Montellano P.R.;
RT "The active site of the thermophilic CYP119 from Sulfolobus solfataricus.";
RL J. Biol. Chem. 275:14112-14123(2000).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-77 AND
RP THR-214.
RX PubMed=12010041; DOI=10.1021/ja017174g;
RA Koo L.S., Immoos C.E., Cohen M.S., Farmer P.J., Ortiz de Montellano P.R.;
RT "Enhanced electron transfer and lauric acid hydroxylation by site-directed
RT mutagenesis of CYP119.";
RL J. Am. Chem. Soc. 124:5684-5691(2002).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18157853; DOI=10.1002/cbic.200700450;
RA Rabe K.S., Kiko K., Niemeyer C.M.;
RT "Characterization of the peroxidase activity of CYP119, a thermostable P450
RT from Sulfolobus acidocaldarius.";
RL ChemBioChem 9:420-425(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH HEME.
RX PubMed=10957637; DOI=10.1107/s0907444900008234;
RA Park S.-Y., Yamane K., Adachi S., Shiro Y., Weiss K.E., Sligar S.G.;
RT "Crystallization and preliminary X-ray diffraction analysis of a cytochrome
RT P450 (CYP119) from Sulfolobus solfataricus.";
RL Acta Crystallogr. D 56:1173-1175(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH HEME.
RX PubMed=10859321; DOI=10.1074/jbc.m004281200;
RA Yano J.K., Koo L.S., Schuller D.J., Li H., Ortiz De Montellano P.R.,
RA Poulos T.L.;
RT "Crystal structure of a thermophilic cytochrome P450 from the archaeon
RT Sulfolobus solfataricus.";
RL J. Biol. Chem. 275:31086-31092(2000).
CC -!- FUNCTION: The endogenous substrate is not known. In vitro, catalyzes
CC the H(2)O(2)-dependent epoxidation of styrene, cis-beta-methylstyrene,
CC and cis-stilbene with retention of stereochemistry. Is able to use
CC cumene hydroperoxide (CHP) or tert-butyl hydroperoxide (TBHP) instead
CC of H(2)O(2) as the electron acceptor. Can also hydroxylate fatty acids
CC such as lauric acid. {ECO:0000269|PubMed:10799487,
CC ECO:0000269|PubMed:12010041, ECO:0000269|PubMed:18157853}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for lauric acid {ECO:0000269|PubMed:10799487,
CC ECO:0000269|PubMed:12010041, ECO:0000269|PubMed:18157853};
CC KM=9.2 mM for styrene {ECO:0000269|PubMed:10799487,
CC ECO:0000269|PubMed:12010041, ECO:0000269|PubMed:18157853};
CC pH dependence:
CC Optimum pH is 8.5 for peroxidase activity.
CC {ECO:0000269|PubMed:10799487, ECO:0000269|PubMed:12010041,
CC ECO:0000269|PubMed:18157853};
CC Temperature dependence:
CC Optimum temperature is about 75 degrees Celsius. Activity is 10-fold
CC greater at 75 degrees Celsius than that measured at 25 degrees
CC Celsius. Thermostable up to 85 degrees Celsius. Thermal denaturation
CC midpoint (Tm) is 91 degrees Celsius. {ECO:0000269|PubMed:10799487,
CC ECO:0000269|PubMed:12010041, ECO:0000269|PubMed:18157853};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:8617361) thought to originate from
CC Sulfolobus solfataricus, but was shown (PubMed:18157853) to stem from
CC Sulfolobus acidocaldarius. This was due to a contamination of the
CC S.solfataricus P1 strain isolate used for the initial cloning with the
CC S.acidocaldarius species. {ECO:0000305|PubMed:18157853,
CC ECO:0000305|PubMed:8617361}.
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DR EMBL; U51337; AAB03278.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY81375.1; -; Genomic_DNA.
DR PIR; S71328; S71328.
DR RefSeq; WP_011278877.1; NC_007181.1.
DR PDB; 1F4T; X-ray; 1.93 A; A/B=1-368.
DR PDB; 1F4U; X-ray; 2.69 A; A/B=1-368.
DR PDB; 1IO7; X-ray; 1.50 A; A/B=1-368.
DR PDB; 1IO8; X-ray; 2.00 A; A/B=1-368.
DR PDB; 1IO9; X-ray; 2.05 A; A/B=1-368.
DR PDB; 4TT5; X-ray; 2.18 A; A=1-368.
DR PDB; 4TUV; X-ray; 2.50 A; A=1-368.
DR PDB; 4WPD; X-ray; 2.00 A; A/B=1-368.
DR PDB; 4WQJ; X-ray; 2.70 A; A=1-368.
DR PDB; 5BV5; X-ray; 2.70 A; A/B/C/D=1-368.
DR PDBsum; 1F4T; -.
DR PDBsum; 1F4U; -.
DR PDBsum; 1IO7; -.
DR PDBsum; 1IO8; -.
DR PDBsum; 1IO9; -.
DR PDBsum; 4TT5; -.
DR PDBsum; 4TUV; -.
DR PDBsum; 4WPD; -.
DR PDBsum; 4WQJ; -.
DR PDBsum; 5BV5; -.
DR AlphaFoldDB; Q55080; -.
DR SMR; Q55080; -.
DR STRING; 330779.Saci_2081; -.
DR PRIDE; Q55080; -.
DR EnsemblBacteria; AAY81375; AAY81375; Saci_2081.
DR GeneID; 3472594; -.
DR KEGG; sai:Saci_2081; -.
DR PATRIC; fig|330779.12.peg.2081; -.
DR eggNOG; arCOG02814; Archaea.
DR HOGENOM; CLU_033716_0_2_2; -.
DR OMA; QEMISTC; -.
DR BRENDA; 1.11.1.7; 6160.
DR EvolutionaryTrace; Q55080; -.
DR Proteomes; UP000001018; Chromosome.
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 GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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 PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase;
KW Oxidoreductase; Peroxidase; Reference proteome.
FT CHAIN 1..368
FT /note="Cytochrome P450 119"
FT /id="PRO_0000052237"
FT BINDING 76
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:10859321,
FT ECO:0000269|PubMed:10957637"
FT BINDING 80
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:10859321,
FT ECO:0000269|PubMed:10957637"
FT BINDING 257
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:10859321,
FT ECO:0000269|PubMed:10957637"
FT BINDING 259
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:10859321,
FT ECO:0000269|PubMed:10957637"
FT BINDING 315
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:10859321,
FT ECO:0000269|PubMed:10957637"
FT BINDING 317
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 MUTAGEN 77
FT /note="D->R: 1.4-fold reduction in styrene epoxidation
FT activity. 13-fold increase in lauric acid hydroxylation
FT activity."
FT /evidence="ECO:0000269|PubMed:12010041"
FT MUTAGEN 213
FT /note="T->A: 1.2-fold reduction in styrene epoxidation
FT activity. No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:10799487"
FT MUTAGEN 213
FT /note="T->F: Loss of styrene epoxidation activity. No
FT effect on thermostability."
FT /evidence="ECO:0000269|PubMed:10799487"
FT MUTAGEN 213
FT /note="T->S: 5-fold reduction in styrene epoxidation
FT activity. No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:10799487"
FT MUTAGEN 213
FT /note="T->V: 147-fold reduction in styrene epoxidation
FT activity. No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:10799487"
FT MUTAGEN 213
FT /note="T->W: 19-fold reduction in styrene epoxidation
FT activity. No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:10799487"
FT MUTAGEN 214
FT /note="T->A: 2.7-fold increase in styrene epoxidation
FT activity. No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:10799487,
FT ECO:0000269|PubMed:12010041"
FT MUTAGEN 214
FT /note="T->V: 3-fold increase in styrene epoxidation
FT activity. 6-fold increase in lauric acid hydroxylation
FT activity. No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:10799487,
FT ECO:0000269|PubMed:12010041"
FT HELIX 2..11
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:1IO7"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:5BV5"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:1IO7"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1IO7"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 89..108
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:1IO7"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 161..178
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1F4T"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1F4T"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 211..227
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:1IO7"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1IO7"
FT TURN 293..296
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1IO7"
FT HELIX 320..335
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 339..348
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:1IO7"
FT STRAND 357..365
FT /evidence="ECO:0007829|PDB:1IO7"
SQ SEQUENCE 368 AA; 42863 MW; E2A5C4F064537E8C CRC64;
MYDWFSEMRK KDPVYYDGNI WQVFSYRYTK EVLNNFSKFS SDLTGYHERL EDLRNGKIRF
DIPTRYTMLT SDPPLHDELR SMSADIFSPQ KLQTLETFIR ETTRSLLDSI DPREDDIVKK
LAVPLPIIVI SKILGLPIED KEKFKEWSDL VAFRLGKPGE IFELGKKYLE LIGYVKDHLN
SGTEVVSRVV NSNLSDIEKL GYIILLLIAG NETTTNLISN SVIDFTRFNL WQRIREENLY
LKAIEEALRY SPPVMRTVRK TKERVKLGDQ TIEEGEYVRV WIASANRDEE VFHDGEKFIP
DRNPNPHLSF GSGIHLCLGA PLARLEARIA IEEFSKRFRH IEILDTEKVP NEVLNGYKRL
VVRLKSNE
