Q55080 (CP119_SULAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome P450 119
EC=1.14.-.-

Alternative name(s):
Peroxidase
EC=1.11.1.7

Gene names

Name:	cyp119
Ordered Locus Names:	Saci_2081

Organism

Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP]

Taxonomic identifier

330779 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length	368 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The endogenous substrate is not known. In vitro, catalyzes the H2O(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 H2O2 as the electron acceptor. Can also hydroxylate fatty acids such as lauric acid. Ref.4 Ref.5 Ref.6
Catalytic activity	2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.
Cofactor	Binds 1 heme group per subunit.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the cytochrome P450 family.
Caution	Was originally (Ref.1) thought to originate from Sulfolobus solfataricus, but was shown (Ref.6) 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.
Biophysicochemical properties	Kinetic parameters: KM=21 µM for lauric acid Ref.4 Ref.5 Ref.6 KM=9.2 mM for styrene pH dependence: Optimum pH is 8.5 for peroxidase activity. 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase Peroxidase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Inferred from electronic annotation. Source: InterPro peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 368

368

Cytochrome P450 119

PRO_0000052237

Sites

Metal binding

317

1

Iron (heme axial ligand)

Binding site

76

1

Heme

Binding site

80

1

Heme

Binding site

257

1

Heme

Binding site

259

1

Heme

Binding site

315

1

Heme

Experimental info

Mutagenesis

77

1

D → R: 1.4-fold reduction in styrene epoxidation activity. 13-fold increase in lauric acid hyroxylation activity. Ref.5

Mutagenesis

213

1

T → A: 1.2-fold reduction in styrene epoxidation activity. No effect on thermostability. Ref.4

Mutagenesis

213

1

T → F: Loss of styrene epoxidation activity. No effect on thermostability. Ref.4

Mutagenesis

213

1

T → S: 5-fold reduction in styrene epoxidation activity. No effect on thermostability. Ref.4

Mutagenesis

213

1

T → V: 147-fold reduction in styrene epoxidation activity. No effect on thermostability. Ref.4

Mutagenesis

213

1

T → W: 19-fold reduction in styrene epoxidation activity. No effect on thermostability. Ref.4

Mutagenesis

214

1

T → A: 2.7-fold increase in styrene epoxidation activity. No effect on thermostability. Ref.4 Ref.5

Mutagenesis

214

1

T → V: 3-fold increase in styrene epoxidation activity. 6-fold increase in lauric acid hyroxylation activity. No effect on thermostability. Ref.4 Ref.5

Secondary structure

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368

Helix Strand Turn

Details...

Helix

2 – 11

10

Beta strand

13 – 16

4

Beta strand

21 – 23

3

Helix

26 – 34

9

Turn

36 – 38

3

Helix

46 – 53

8

Turn

54 – 56

3

Helix

63 – 65

3

Helix

68 – 70

3

Helix

75 – 80

6

Helix

81 – 83

3

Turn

84 – 87

4

Helix

89 – 108

20

Beta strand

114 – 116

3

Helix

117 – 120

4

Turn

121 – 123

3

Helix

124 – 134

11

Helix

138 – 140

3

Helix

141 – 147

7

Helix

148 – 150

3

Helix

161 – 178

18

Helix

184 – 190

7

Helix

196 – 208

13

Helix

211 – 227

17

Helix

231 – 237

7

Helix

240 – 250

11

Beta strand

257 – 263

7

Beta strand

265 – 267

3

Beta strand

270 – 272

3

Beta strand

277 – 280

4

Helix

282 – 285

4

Turn

289 – 291

3

Turn

293 – 296

4

Helix

313 – 315

3

Helix

320 – 335

16

Beta strand

339 – 348

10

Beta strand

352 – 354

3

Beta strand

357 – 365

9

Sequences

	Sequence		Length	Mass (Da)
	Q55080 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E2A5C4F064537E8C	FASTA	368	42,863
	10 20 30 40 50 60 MYDWFSEMRK KDPVYYDGNI WQVFSYRYTK EVLNNFSKFS SDLTGYHERL EDLRNGKIRF 70 80 90 100 110 120 DIPTRYTMLT SDPPLHDELR SMSADIFSPQ KLQTLETFIR ETTRSLLDSI DPREDDIVKK 130 140 150 160 170 180 LAVPLPIIVI SKILGLPIED KEKFKEWSDL VAFRLGKPGE IFELGKKYLE LIGYVKDHLN 190 200 210 220 230 240 SGTEVVSRVV NSNLSDIEKL GYIILLLIAG NETTTNLISN SVIDFTRFNL WQRIREENLY 250 260 270 280 290 300 LKAIEEALRY SPPVMRTVRK TKERVKLGDQ TIEEGEYVRV WIASANRDEE VFHDGEKFIP 310 320 330 340 350 360 DRNPNPHLSF GSGIHLCLGA PLARLEARIA IEEFSKRFRH IEILDTEKVP NEVLNGYKRL VVRLKSNE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a potential cytochrome P450 from the archaeon Sulfolobus solfataricus." Wright R.L., Harris K., Solow B., White R.H., Kennelly R.H. FEBS Lett. 384:235-239(1996) [PubMed: 8617361] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota." Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A. J. Bacteriol. 187:4992-4999(2005) [PubMed: 15995215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.
[3]	"Characterization of a cytochrome P450 from the acidothermophilic archaea Sulfolobus solfataricus." McLean M.A., Maves S.A., Weiss K.E., Krepich S., Sligar S.G. Biochem. Biophys. Res. Commun. 252:166-172(1998) [PubMed: 9813164] [Abstract] Cited for: CHARACTERIZATION.
[4]	"The active site of the thermophilic CYP119 from Sulfolobus solfataricus." Koo L.S., Tschirret-Guth R.A., Straub W.E., Moenne-Loccoz P., Loehr T.M., Ortiz de Montellano P.R. J. Biol. Chem. 275:14112-14123(2000) [PubMed: 10799487] [Abstract] Cited for: FUNCTION, HEME BINDING, REACTION STEREOCHEMISTRY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF THR-213 AND THR-214.
[5]	"Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119." Koo L.S., Immoos C.E., Cohen M.S., Farmer P.J., Ortiz de Montellano P.R. J. Am. Chem. Soc. 124:5684-5691(2002) [PubMed: 12010041] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-77 AND THR-214.
[6]	"Characterization of the peroxidase activity of CYP119, a thermostable P450 from Sulfolobus acidocaldarius." Rabe K.S., Kiko K., Niemeyer C.M. ChemBioChem 9:420-425(2008) [PubMed: 18157853] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[7]	"Crystallization and preliminary X-ray diffraction analysis of a cytochrome P450 (CYP119) from Sulfolobus solfataricus." Park S.-Y., Yamane K., Adachi S., Shiro Y., Weiss K.E., Sligar S.G. Acta Crystallogr. D 56:1173-1175(2000) [PubMed: 10957637] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMLEX WITH HEME.
[8]	"Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus." Yano J.K., Koo L.S., Schuller D.J., Li H., Ortiz De Montellano P.R., Poulos T.L. J. Biol. Chem. 275:31086-31092(2000) [PubMed: 10859321] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH HEME.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U51337 Genomic DNA. Translation: AAB03278.1.
CP000077 Genomic DNA. Translation: AAY81375.1.

PIR

S71328.

RefSeq

YP_256668.1. NC_007181.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F4T	X-ray	1.93	A/B	1-368	[»]
1F4U	X-ray	2.69	A/B	1-368	[»]
1IO7	X-ray	1.50	A/B	1-368	[»]
1IO8	X-ray	2.00	A/B	1-368	[»]
1IO9	X-ray	2.05	A/B	1-368	[»]

ProteinModelPortal

Q55080.

SMR

Q55080. Positions 1-367.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3472594.

GenomeReviews

Gene locus Saci_2081 in contig CP000077_GR.

KEGG

sai:Saci_2081.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG695262.

OMA

PPLHDEL.

ProtClustDB

CLSK268599.

Family and domain databases

InterPro

IPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]

Gene3D

G3DSA:1.10.630.10. Cyt_P450. 1 hit.

KO

K00495.

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00359. BP450.
PR00385. P450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CP119_SULAC

Accession

Primary (citable) accession number: Q55080
Secondary accession number(s): Q4J756

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	November 16, 2011
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program