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Fatty-acid peroxygenase (EC 1.11.2.4) (Cytochrome P450 152A1) (Cytochrome P450BsBeta) (Fatty acid beta-hydroxylase)

 CYPC_BACSU              Reviewed;         417 AA.
O31440;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 128.
RecName: Full=Fatty-acid peroxygenase;
EC=1.11.2.4;
AltName: Full=Cytochrome P450 152A1;
AltName: Full=Cytochrome P450BsBeta;
AltName: Full=Fatty acid beta-hydroxylase;
Name=cypC; Synonyms=CYP152A1; OrderedLocusNames=BSU02100;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
"Sequence analysis of the 70kb region between 17 and 23 degree of the
Bacillus subtilis chromosome.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, CATALYTIC ACTIVITY,
AND FUNCTION.
STRAIN=NBRC 14144 / BSF 11;
PubMed=10529095; DOI=10.1007/s11745-999-0431-3;
Matsunaga I., Ueda A., Fujiwara N., Sumimoto T., Ichihara K.;
"Characterization of the ybdT gene product of Bacillus subtilis: novel
fatty acid beta-hydroxylating cytochrome P450.";
Lipids 34:841-846(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND RESONANCE RAMAN
SPECTROSCOPY.
PubMed=12519760; DOI=10.1074/jbc.M211575200;
Lee D.-S., Yamada A., Sugimoto H., Matsunaga I., Ogura H.,
Ichihara K., Adachi S., Park S.-Y., Shiro Y.;
"Substrate recognition and molecular mechanism of fatty acid
hydroxylation by cytochrome P450 from Bacillus subtilis:
crystallographic, spectroscopic and mutational studies.";
J. Biol. Chem. 278:9761-9767(2003).
-!- FUNCTION: Catalyzes the alpha- and beta-hydroxylation of myristic
acid in the presence of hydrogen peroxide.
{ECO:0000269|PubMed:10529095}.
-!- CATALYTIC ACTIVITY: Fatty acid + H(2)O(2) = 3- or 2-hydroxy fatty
acid + H(2)O. {ECO:0000269|PubMed:10529095}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB006424; BAA33107.1; -; Genomic_DNA.
EMBL; AL009126; CAB12004.1; -; Genomic_DNA.
PIR; C69748; C69748.
RefSeq; NP_388092.1; NC_000964.3.
RefSeq; WP_003246284.1; NZ_JNCM01000030.1.
PDB; 1IZO; X-ray; 2.10 A; A/B/C=1-417.
PDB; 2ZQJ; X-ray; 2.90 A; A/B/C=1-417.
PDB; 2ZQX; X-ray; 2.37 A; A/B/C=1-417.
PDBsum; 1IZO; -.
PDBsum; 2ZQJ; -.
PDBsum; 2ZQX; -.
ProteinModelPortal; O31440; -.
SMR; O31440; -.
STRING; 224308.Bsubs1_010100001173; -.
DrugBank; DB04257; Palmitoleic Acid.
SwissLipids; SLP:000001181; -.
PaxDb; O31440; -.
EnsemblBacteria; CAB12004; CAB12004; BSU02100.
GeneID; 938449; -.
KEGG; bsu:BSU02100; -.
PATRIC; fig|224308.179.peg.216; -.
eggNOG; ENOG4107E6A; Bacteria.
eggNOG; COG2124; LUCA.
HOGENOM; HOG000099453; -.
InParanoid; O31440; -.
KO; K15629; -.
OMA; MFVQEVR; -.
PhylomeDB; O31440; -.
BioCyc; BSUB:BSU02100-MONOMER; -.
BioCyc; MetaCyc:BSU02100-MONOMER; -.
BRENDA; 1.11.2.4; 658.
EvolutionaryTrace; O31440; -.
Proteomes; UP000001570; Chromosome.
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.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
SUPFAM; SSF48264; SSF48264; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Heme; Iron; Metal-binding;
Monooxygenase; Oxidoreductase; Reference proteome.
CHAIN 1 417 Fatty-acid peroxygenase.
/FTId=PRO_0000052235.
METAL 363 363 Iron (heme axial ligand).
HELIX 13 20 {ECO:0000244|PDB:1IZO}.
HELIX 21 23 {ECO:0000244|PDB:1IZO}.
HELIX 24 31 {ECO:0000244|PDB:1IZO}.
STRAND 34 41 {ECO:0000244|PDB:1IZO}.
STRAND 44 49 {ECO:0000244|PDB:1IZO}.
HELIX 52 58 {ECO:0000244|PDB:1IZO}.
TURN 61 63 {ECO:0000244|PDB:1IZO}.
HELIX 72 75 {ECO:0000244|PDB:1IZO}.
TURN 76 79 {ECO:0000244|PDB:1IZO}.
HELIX 84 86 {ECO:0000244|PDB:1IZO}.
HELIX 89 101 {ECO:0000244|PDB:1IZO}.
HELIX 105 126 {ECO:0000244|PDB:1IZO}.
STRAND 129 133 {ECO:0000244|PDB:1IZO}.
HELIX 134 150 {ECO:0000244|PDB:1IZO}.
TURN 156 158 {ECO:0000244|PDB:1IZO}.
HELIX 159 172 {ECO:0000244|PDB:1IZO}.
HELIX 178 202 {ECO:0000244|PDB:1IZO}.
HELIX 213 219 {ECO:0000244|PDB:1IZO}.
HELIX 230 245 {ECO:0000244|PDB:1IZO}.
HELIX 247 260 {ECO:0000244|PDB:1IZO}.
HELIX 263 269 {ECO:0000244|PDB:1IZO}.
HELIX 273 286 {ECO:0000244|PDB:1IZO}.
STRAND 292 297 {ECO:0000244|PDB:1IZO}.
STRAND 301 303 {ECO:0000244|PDB:1IZO}.
STRAND 306 308 {ECO:0000244|PDB:1IZO}.
STRAND 313 317 {ECO:0000244|PDB:1IZO}.
HELIX 318 322 {ECO:0000244|PDB:1IZO}.
TURN 325 327 {ECO:0000244|PDB:1IZO}.
STRAND 328 330 {ECO:0000244|PDB:1IZO}.
HELIX 336 339 {ECO:0000244|PDB:1IZO}.
STRAND 346 348 {ECO:0000244|PDB:1IZO}.
STRAND 359 361 {ECO:0000244|PDB:1IZO}.
HELIX 366 382 {ECO:0000244|PDB:1IZO}.
STRAND 384 387 {ECO:0000244|PDB:1IZO}.
STRAND 397 401 {ECO:0000244|PDB:1IZO}.
STRAND 409 415 {ECO:0000244|PDB:1IZO}.
SEQUENCE 417 AA; 48109 MW; 252C0684E85CDCED CRC64;
MNEQIPHDKS LDNSLTLLKE GYLFIKNRTE RYNSDLFQAR LLGKNFICMT GAEAAKVFYD
TDRFQRQNAL PKRVQKSLFG VNAIQGMDGS AHIHRKMLFL SLMTPPHQKR LAELMTEEWK
AAVTRWEKAD EVVLFEEAKE ILCRVACYWA GVPLKETEVK ERADDFIDMV DAFGAVGPRH
WKGRRARPRA EEWIEVMIED ARAGLLKTTS GTALHEMAFH TQEDGSQLDS RMAAIELINV
LRPIVAISYF LVFSALALHE HPKYKEWLRS GNSREREMFV QEVRRYYPFG PFLGALVKKD
FVWNNCEFKK GTSVLLDLYG TNHDPRLWDH PDEFRPERFA EREENLFDMI PQGGGHAEKG
HRCPGEGITI EVMKASLDFL VHQIEYDVPE QSLHYSLARM PSLPESGFVM SGIRRKS


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