CP119_SULTO
ID CP119_SULTO Reviewed; 367 AA.
AC Q972I2; F9VNW4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cytochrome P450 119;
DE EC=1.14.-.-;
GN Name=cyp119; OrderedLocusNames=STK_11480;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH HEME, AND TEMPERATURE
RP DEPENDENCE.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=15219985; DOI=10.1016/j.jinorgbio.2004.05.002;
RA Oku Y., Ohtaki A., Kamitori S., Nakamura N., Yohda M., Ohno H.,
RA Kawarabayasi Y.;
RT "Structure and direct electrochemistry of cytochrome P450 from the
RT thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain 7.";
RL J. Inorg. Biochem. 98:1194-1199(2004).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Active up to 80 degrees Celsius. Thermostable.
CC {ECO:0000269|PubMed:15219985};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; BA000023; BAK54472.1; -; Genomic_DNA.
DR RefSeq; WP_010979165.1; NC_003106.2.
DR PDB; 1UE8; X-ray; 3.00 A; A=1-367.
DR PDB; 3B4X; X-ray; 1.94 A; A=1-367.
DR PDBsum; 1UE8; -.
DR PDBsum; 3B4X; -.
DR AlphaFoldDB; Q972I2; -.
DR SMR; Q972I2; -.
DR STRING; 273063.STK_11480; -.
DR EnsemblBacteria; BAK54472; BAK54472; STK_11480.
DR GeneID; 1459138; -.
DR KEGG; sto:STK_11480; -.
DR PATRIC; fig|273063.9.peg.1301; -.
DR eggNOG; arCOG02814; Archaea.
DR OMA; QEMISTC; -.
DR OrthoDB; 18779at2157; -.
DR BRENDA; 1.11.2.1; 15396.
DR BRENDA; 1.14.13.B28; 15396.
DR EvolutionaryTrace; Q972I2; -.
DR Proteomes; UP000001015; 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 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; Reference proteome.
FT CHAIN 1..367
FT /note="Cytochrome P450 119"
FT /id="PRO_0000343614"
FT BINDING 76
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:15219985"
FT BINDING 257
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:15219985"
FT BINDING 315
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:15219985"
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 HELIX 2..11
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:3B4X"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:3B4X"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:3B4X"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:3B4X"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 162..178
FT /evidence="ECO:0007829|PDB:3B4X"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:3B4X"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 213..228
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:3B4X"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:3B4X"
FT HELIX 320..337
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 338..348
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:3B4X"
FT STRAND 356..366
FT /evidence="ECO:0007829|PDB:3B4X"
SQ SEQUENCE 367 AA; 42324 MW; E001CB1FF8BA8E8C CRC64;
MYDWFKQMRK ESPVYYDGKV WNLFKYEDCK MVLNDHKRFS SNLTGYNDKL EMLRSGKVFF
DIPTRYTMLT SDPPLHDELR NLTADAFNPS NLPVDFVREV TVKLLSELDE EFDVIESFAI
PLPILVISKM LGINPDVKKV KDWSDLVALR LGRADEIFSI GRKYLELISF SKKELDSRKG
KEIVDLTGKI ANSNLSELEK EGYFILLMIA GNETTTNLIG NAIEDFTLYN SWDYVREKGA
LKAVEEALRF SPPVMRTIRV TKEKVKIRDQ VIDEGELVRV WIASANRDEE VFKDPDSFIP
DRTPNPHLSF GSGIHLCLGA PLARLEARIA LEEFAKKFRV KEIVKKEKID NEVLNGYRKL
VVRVERA
