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Cytochrome P450 119 (EC 1.14.-.-) (Peroxidase) (EC 1.11.1.7)

 CP119_SULAC             Reviewed;         368 AA.
Q55080; Q4J756;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 117.
RecName: Full=Cytochrome P450 119;
EC=1.14.-.-;
AltName: Full=Peroxidase;
EC=1.11.1.7;
Name=cyp119; OrderedLocusNames=Saci_2081;
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 /
NBRC 15157 / NCIMB 11770).
Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
Sulfolobus.
NCBI_TaxID=330779;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8617361; DOI=10.1016/0014-5793(96)00322-5;
Wright R.L., Harris K., Solow B., White R.H., Kennelly R.H.;
"Cloning of a potential cytochrome P450 from the archaeon Sulfolobus
solfataricus.";
FEBS Lett. 384:235-239(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
"The genome of Sulfolobus acidocaldarius, a model organism of the
Crenarchaeota.";
J. Bacteriol. 187:4992-4999(2005).
[3]
CHARACTERIZATION.
PubMed=9813164; DOI=10.1006/bbrc.1998.9584;
McLean M.A., Maves S.A., Weiss K.E., Krepich S., Sligar S.G.;
"Characterization of a cytochrome P450 from the acidothermophilic
archaea Sulfolobus solfataricus.";
Biochem. Biophys. Res. Commun. 252:166-172(1998).
[4]
FUNCTION, HEME BINDING, REACTION STEREOCHEMISTRY, BIOPHYSICOCHEMICAL
PROPERTIES, AND MUTAGENESIS OF THR-213 AND THR-214.
PubMed=10799487; DOI=10.1074/jbc.275.19.14112;
Koo L.S., Tschirret-Guth R.A., Straub W.E., Moenne-Loccoz P.,
Loehr T.M., Ortiz de Montellano P.R.;
"The active site of the thermophilic CYP119 from Sulfolobus
solfataricus.";
J. Biol. Chem. 275:14112-14123(2000).
[5]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-77 AND
THR-214.
PubMed=12010041; DOI=10.1021/ja017174g;
Koo L.S., Immoos C.E., Cohen M.S., Farmer P.J.,
Ortiz de Montellano P.R.;
"Enhanced electron transfer and lauric acid hydroxylation by site-
directed mutagenesis of CYP119.";
J. Am. Chem. Soc. 124:5684-5691(2002).
[6]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18157853; DOI=10.1002/cbic.200700450;
Rabe K.S., Kiko K., Niemeyer C.M.;
"Characterization of the peroxidase activity of CYP119, a thermostable
P450 from Sulfolobus acidocaldarius.";
ChemBioChem 9:420-425(2008).
[7]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH HEME.
PubMed=10957637; DOI=10.1107/S0907444900008234;
Park S.-Y., Yamane K., Adachi S., Shiro Y., Weiss K.E., Sligar S.G.;
"Crystallization and preliminary X-ray diffraction analysis of a
cytochrome P450 (CYP119) from Sulfolobus solfataricus.";
Acta Crystallogr. D 56:1173-1175(2000).
[8]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH HEME.
PubMed=10859321; DOI=10.1074/jbc.M004281200;
Yano J.K., Koo L.S., Schuller D.J., Li H., Ortiz De Montellano P.R.,
Poulos T.L.;
"Crystal structure of a thermophilic cytochrome P450 from the archaeon
Sulfolobus solfataricus.";
J. Biol. Chem. 275:31086-31092(2000).
-!- FUNCTION: The endogenous substrate is not known. In vitro,
catalyzes the H(2)O(2)-dependent epoxidation of styrene, cis-beta-
methylstyrene, and cis-stilbene with retention of stereochemistry.
Is able to use cumene hydroperoxide (CHP) or tert-butyl
hydroperoxide (TBHP) instead of H(2)O(2) as the electron acceptor.
Can also hydroxylate fatty acids such as lauric acid.
{ECO:0000269|PubMed:10799487, ECO:0000269|PubMed:12010041,
ECO:0000269|PubMed:18157853}.
-!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl
radical of the donor + 2 H(2)O.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Note=Binds 1 heme group per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=21 uM for lauric acid {ECO:0000269|PubMed:10799487,
ECO:0000269|PubMed:12010041, ECO:0000269|PubMed:18157853};
KM=9.2 mM for styrene {ECO:0000269|PubMed:10799487,
ECO:0000269|PubMed:12010041, ECO:0000269|PubMed:18157853};
pH dependence:
Optimum pH is 8.5 for peroxidase activity.
{ECO:0000269|PubMed:10799487, ECO:0000269|PubMed:12010041,
ECO:0000269|PubMed:18157853};
Temperature dependence:
Optimum temperature is about 75 degrees Celsius. Activity is 10-
fold greater at 75 degrees Celsius than that measured at 25
degrees Celsius. Thermostable up to 85 degrees Celsius. Thermal
denaturation midpoint (Tm) is 91 degrees Celsius.
{ECO:0000269|PubMed:10799487, ECO:0000269|PubMed:12010041,
ECO:0000269|PubMed:18157853};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- CAUTION: Was originally (PubMed:8617361) thought to originate from
Sulfolobus solfataricus, but was shown (PubMed:18157853) to stem
from Sulfolobus acidocaldarius. This was due to a contamination of
the S.solfataricus P1 strain isolate used for the initial cloning
with the S.acidocaldarius species. {ECO:0000305|PubMed:18157853,
ECO:0000305|PubMed:8617361}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U51337; AAB03278.1; -; Genomic_DNA.
EMBL; CP000077; AAY81375.1; -; Genomic_DNA.
PIR; S71328; S71328.
RefSeq; WP_011278877.1; NC_007181.1.
PDB; 1F4T; X-ray; 1.93 A; A/B=1-368.
PDB; 1F4U; X-ray; 2.69 A; A/B=1-368.
PDB; 1IO7; X-ray; 1.50 A; A/B=1-368.
PDB; 1IO8; X-ray; 2.00 A; A/B=1-368.
PDB; 1IO9; X-ray; 2.05 A; A/B=1-368.
PDB; 4TT5; X-ray; 2.18 A; A=1-368.
PDB; 4TUV; X-ray; 2.50 A; A=1-368.
PDB; 4WPD; X-ray; 2.00 A; A/B=1-368.
PDB; 4WQJ; X-ray; 2.70 A; A=1-368.
PDB; 5BV5; X-ray; 2.70 A; A/B/C/D=1-368.
PDBsum; 1F4T; -.
PDBsum; 1F4U; -.
PDBsum; 1IO7; -.
PDBsum; 1IO8; -.
PDBsum; 1IO9; -.
PDBsum; 4TT5; -.
PDBsum; 4TUV; -.
PDBsum; 4WPD; -.
PDBsum; 4WQJ; -.
PDBsum; 5BV5; -.
ProteinModelPortal; Q55080; -.
SMR; Q55080; -.
STRING; 330779.Saci_2081; -.
PRIDE; Q55080; -.
EnsemblBacteria; AAY81375; AAY81375; Saci_2081.
GeneID; 3472594; -.
KEGG; sai:Saci_2081; -.
PATRIC; fig|330779.12.peg.2081; -.
eggNOG; arCOG02814; Archaea.
eggNOG; COG2124; LUCA.
HOGENOM; HOG000243678; -.
KO; K21201; -.
OMA; EEIKWQG; -.
OrthoDB; POG093Z029Q; -.
BRENDA; 1.11.1.7; 6160.
EvolutionaryTrace; Q55080; -.
Proteomes; UP000001018; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR002397; Cyt_P450_B.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00359; BP450.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Heme; Iron; Metal-binding;
Monooxygenase; Oxidoreductase; Peroxidase; Reference proteome.
CHAIN 1 368 Cytochrome P450 119.
/FTId=PRO_0000052237.
METAL 317 317 Iron (heme axial ligand).
BINDING 76 76 Heme. {ECO:0000269|PubMed:10859321,
ECO:0000269|PubMed:10957637}.
BINDING 80 80 Heme. {ECO:0000269|PubMed:10859321,
ECO:0000269|PubMed:10957637}.
BINDING 257 257 Heme. {ECO:0000269|PubMed:10859321,
ECO:0000269|PubMed:10957637}.
BINDING 259 259 Heme. {ECO:0000269|PubMed:10859321,
ECO:0000269|PubMed:10957637}.
BINDING 315 315 Heme. {ECO:0000269|PubMed:10859321,
ECO:0000269|PubMed:10957637}.
MUTAGEN 77 77 D->R: 1.4-fold reduction in styrene
epoxidation activity. 13-fold increase in
lauric acid hydroxylation activity.
{ECO:0000269|PubMed:12010041}.
MUTAGEN 213 213 T->A: 1.2-fold reduction in styrene
epoxidation activity. No effect on
thermostability.
{ECO:0000269|PubMed:10799487}.
MUTAGEN 213 213 T->F: Loss of styrene epoxidation
activity. No effect on thermostability.
{ECO:0000269|PubMed:10799487}.
MUTAGEN 213 213 T->S: 5-fold reduction in styrene
epoxidation activity. No effect on
thermostability.
{ECO:0000269|PubMed:10799487}.
MUTAGEN 213 213 T->V: 147-fold reduction in styrene
epoxidation activity. No effect on
thermostability.
{ECO:0000269|PubMed:10799487}.
MUTAGEN 213 213 T->W: 19-fold reduction in styrene
epoxidation activity. No effect on
thermostability.
{ECO:0000269|PubMed:10799487}.
MUTAGEN 214 214 T->A: 2.7-fold increase in styrene
epoxidation activity. No effect on
thermostability.
{ECO:0000269|PubMed:10799487,
ECO:0000269|PubMed:12010041}.
MUTAGEN 214 214 T->V: 3-fold increase in styrene
epoxidation activity. 6-fold increase in
lauric acid hydroxylation activity. No
effect on thermostability.
{ECO:0000269|PubMed:10799487,
ECO:0000269|PubMed:12010041}.
HELIX 2 11 {ECO:0000244|PDB:1IO7}.
STRAND 13 16 {ECO:0000244|PDB:1IO7}.
STRAND 21 23 {ECO:0000244|PDB:1IO7}.
HELIX 26 34 {ECO:0000244|PDB:1IO7}.
TURN 36 38 {ECO:0000244|PDB:1IO7}.
STRAND 39 41 {ECO:0000244|PDB:5BV5}.
HELIX 46 53 {ECO:0000244|PDB:1IO7}.
TURN 54 56 {ECO:0000244|PDB:1IO7}.
HELIX 63 65 {ECO:0000244|PDB:1IO7}.
HELIX 68 70 {ECO:0000244|PDB:1IO7}.
HELIX 75 80 {ECO:0000244|PDB:1IO7}.
HELIX 81 83 {ECO:0000244|PDB:1IO7}.
TURN 84 87 {ECO:0000244|PDB:1IO7}.
HELIX 89 108 {ECO:0000244|PDB:1IO7}.
STRAND 114 116 {ECO:0000244|PDB:1IO7}.
HELIX 117 120 {ECO:0000244|PDB:1IO7}.
TURN 121 123 {ECO:0000244|PDB:1IO7}.
HELIX 124 134 {ECO:0000244|PDB:1IO7}.
HELIX 138 140 {ECO:0000244|PDB:1IO7}.
HELIX 141 147 {ECO:0000244|PDB:1IO7}.
HELIX 148 150 {ECO:0000244|PDB:1IO7}.
HELIX 161 178 {ECO:0000244|PDB:1IO7}.
HELIX 179 181 {ECO:0000244|PDB:1F4T}.
HELIX 184 190 {ECO:0000244|PDB:1IO7}.
STRAND 192 194 {ECO:0000244|PDB:1F4T}.
HELIX 196 208 {ECO:0000244|PDB:1IO7}.
HELIX 211 227 {ECO:0000244|PDB:1IO7}.
HELIX 231 237 {ECO:0000244|PDB:1IO7}.
HELIX 240 250 {ECO:0000244|PDB:1IO7}.
STRAND 257 263 {ECO:0000244|PDB:1IO7}.
STRAND 265 267 {ECO:0000244|PDB:1IO7}.
STRAND 270 272 {ECO:0000244|PDB:1IO7}.
STRAND 277 280 {ECO:0000244|PDB:1IO7}.
HELIX 282 285 {ECO:0000244|PDB:1IO7}.
TURN 289 291 {ECO:0000244|PDB:1IO7}.
TURN 293 296 {ECO:0000244|PDB:1IO7}.
HELIX 313 315 {ECO:0000244|PDB:1IO7}.
HELIX 320 335 {ECO:0000244|PDB:1IO7}.
STRAND 339 348 {ECO:0000244|PDB:1IO7}.
STRAND 352 354 {ECO:0000244|PDB:1IO7}.
STRAND 357 365 {ECO:0000244|PDB:1IO7}.
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


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