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 03-AUG-2022, entry version 146.
DE RecName: Full=Fatty-acid peroxygenase;
DE EC=1.11.2.4 {ECO:0000269|PubMed:10529095};
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] {ECO:0007744|PDB:1IZO}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH HEME, RESONANCE RAMAN
RP SPECTROSCOPY, AND COFACTOR.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48361;
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48385;
CC Evidence={ECO:0000269|PubMed:10529095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + tetradecanoate = (3R)-hydroxytetradecanoate + H2O;
CC Xref=Rhea:RHEA:46024, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:85635; EC=1.11.2.4;
CC Evidence={ECO:0000269|PubMed:10529095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46025;
CC Evidence={ECO:0000269|PubMed:10529095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + tetradecanoate = (2R)-hydroxytetradecanoate + H2O;
CC Xref=Rhea:RHEA:46028, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:85636; EC=1.11.2.4;
CC Evidence={ECO:0000269|PubMed:10529095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46029;
CC Evidence={ECO:0000269|PubMed:10529095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + tetradecanoate = (2S)-hydroxytetradecanoate + H2O;
CC Xref=Rhea:RHEA:46032, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:85637; EC=1.11.2.4;
CC Evidence={ECO:0000269|PubMed:10529095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46033;
CC Evidence={ECO:0000269|PubMed:10529095};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:12519760};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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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 AlphaFoldDB; O31440; -.
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; BSU_02100.
DR GeneID; 938449; -.
DR KEGG; bsu:BSU02100; -.
DR PATRIC; fig|224308.179.peg.216; -.
DR eggNOG; COG2124; Bacteria.
DR InParanoid; O31440; -.
DR OMA; GPRHWRA; -.
DR PhylomeDB; O31440; -.
DR BioCyc; BSUB:BSU02100-MON; -.
DR BioCyc; MetaCyc:BSU02100-MON; -.
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;
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 BINDING 363
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 /evidence="ECO:0000269|PubMed:12519760"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:1IZO"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:1IZO"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 105..126
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:1IZO"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 178..202
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 230..245
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:1IZO"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1IZO"
FT HELIX 366..382
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 397..401
FT /evidence="ECO:0007829|PDB:1IZO"
FT STRAND 409..415
FT /evidence="ECO:0007829|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
