(data stored in ACNUC7421 zone)

SWISSPROT: CYPC_BACSU

ID   CYPC_BACSU              Reviewed;         417 AA.
AC   O31440;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-DEC-2019, entry version 136.
DE   RecName: Full=Fatty-acid peroxygenase;
DE            EC=1.11.2.4;
DE   AltName: Full=Cytochrome P450 152A1;
DE   AltName: Full=Cytochrome P450BsBeta;
DE   AltName: Full=Fatty acid beta-hydroxylase;
GN   Name=cypC; Synonyms=CYP152A1; OrderedLocusNames=BSU02100;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT   "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT   Bacillus subtilis chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, CATALYTIC ACTIVITY, AND
RP   FUNCTION.
RC   STRAIN=NBRC 14144 / BSF 11;
RX   PubMed=10529095; DOI=10.1007/s11745-999-0431-3;
RA   Matsunaga I., Ueda A., Fujiwara N., Sumimoto T., Ichihara K.;
RT   "Characterization of the ybdT gene product of Bacillus subtilis: novel
RT   fatty acid beta-hydroxylating cytochrome P450.";
RL   Lipids 34:841-846(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND RESONANCE RAMAN SPECTROSCOPY.
RX   PubMed=12519760; DOI=10.1074/jbc.m211575200;
RA   Lee D.-S., Yamada A., Sugimoto H., Matsunaga I., Ogura H., Ichihara K.,
RA   Adachi S., Park S.-Y., Shiro Y.;
RT   "Substrate recognition and molecular mechanism of fatty acid hydroxylation
RT   by cytochrome P450 from Bacillus subtilis: crystallographic, spectroscopic
RT   and mutational studies.";
RL   J. Biol. Chem. 278:9761-9767(2003).
CC   -!- FUNCTION: Catalyzes the alpha- and beta-hydroxylation of myristic acid
CC       in the presence of hydrogen peroxide. {ECO:0000269|PubMed:10529095}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-saturated fatty acid + H2O2 = a 2-hydroxy fatty acid +
CC         H2O; Xref=Rhea:RHEA:48360, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:76176, ChEBI:CHEBI:83955; EC=1.11.2.4;
CC         Evidence={ECO:0000269|PubMed:10529095};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-saturated fatty acid + H2O2 = 3-hydroxy fatty acid + H2O;
CC         Xref=Rhea:RHEA:48384, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:76928, ChEBI:CHEBI:84196; EC=1.11.2.4;
CC         Evidence={ECO:0000269|PubMed:10529095};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
DR   EMBL; AB006424; BAA33107.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12004.1; -; Genomic_DNA.
DR   PIR; C69748; C69748.
DR   RefSeq; NP_388092.1; NC_000964.3.
DR   RefSeq; WP_003246284.1; NZ_JNCM01000030.1.
DR   PDB; 1IZO; X-ray; 2.10 A; A/B/C=1-417.
DR   PDB; 2ZQJ; X-ray; 2.90 A; A/B/C=1-417.
DR   PDB; 2ZQX; X-ray; 2.37 A; A/B/C=1-417.
DR   PDBsum; 1IZO; -.
DR   PDBsum; 2ZQJ; -.
DR   PDBsum; 2ZQX; -.
DR   SMR; O31440; -.
DR   STRING; 224308.BSU02100; -.
DR   DrugBank; DB04257; Palmitoleic Acid.
DR   SwissLipids; SLP:000001181; -.
DR   PaxDb; O31440; -.
DR   PRIDE; O31440; -.
DR   EnsemblBacteria; CAB12004; CAB12004; BSU02100.
DR   GeneID; 938449; -.
DR   KEGG; bsu:BSU02100; -.
DR   PATRIC; fig|224308.179.peg.216; -.
DR   eggNOG; ENOG4107E6A; Bacteria.
DR   eggNOG; COG2124; LUCA.
DR   HOGENOM; HOG000099453; -.
DR   InParanoid; O31440; -.
DR   KO; K15629; -.
DR   OMA; MFVQEVR; -.
DR   PhylomeDB; O31440; -.
DR   BioCyc; BSUB:BSU02100-MONOMER; -.
DR   BioCyc; MetaCyc:BSU02100-MONOMER; -.
DR   BRENDA; 1.11.2.4; 658.
DR   EvolutionaryTrace; O31440; -.
DR   Proteomes; UP000001570; Chromosome.
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; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O31440.
DR   SWISS-2DPAGE; O31440.
KW   3D-structure; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..417
FT                   /note="Fatty-acid peroxygenase"
FT                   /id="PRO_0000052235"
FT   METAL           363
FT                   /note="Iron (heme axial ligand)"
FT   HELIX           13..20
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           21..23
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           24..31
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          34..41
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          44..49
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           52..58
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   TURN            61..63
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           72..75
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   TURN            76..79
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           84..86
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           89..101
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           105..126
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          129..133
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           134..150
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   TURN            156..158
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           159..172
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           178..202
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           213..219
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           230..245
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           247..260
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           263..269
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           273..286
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          292..297
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          301..303
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          306..308
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          313..317
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           318..322
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   TURN            325..327
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          328..330
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           336..339
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          346..348
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          359..361
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   HELIX           366..382
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          384..387
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          397..401
FT                   /evidence="ECO:0000244|PDB:1IZO"
FT   STRAND          409..415
FT                   /evidence="ECO:0000244|PDB:1IZO"
SQ   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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