CYPC_BACMM
ID CYPC_BACMM Reviewed; 419 AA.
AC I3DZK9;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Fatty-acid peroxygenase {ECO:0000305|PubMed:30119014};
DE EC=1.11.2.4 {ECO:0000269|PubMed:30119014};
DE AltName: Full=Cytochrome P450 peroxygenase CYP152K6 {ECO:0000303|PubMed:30119014};
GN Name=cypC {ECO:0000312|EMBL:AIE59747.1};
GN Synonyms=CYP152K6 {ECO:0000303|PubMed:30119014};
GN ORFNames=BMMGA3_06595 {ECO:0000312|EMBL:AIE59747.1};
OS Bacillus methanolicus (strain MGA3 / ATCC 53907).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=796606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGA3 / ATCC 53907;
RX PubMed=25758049; DOI=10.1186/s12864-015-1239-4;
RA Irla M., Neshat A., Brautaset T., Ruckert C., Kalinowski J., Wendisch V.F.;
RT "Transcriptome analysis of thermophilic methylotrophic Bacillus
RT methanolicus MGA3 using RNA-sequencing provides detailed insights into its
RT previously uncharted transcriptional landscape.";
RL BMC Genomics 16:73-73(2015).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH HEME AND
RP TETRADECANOATE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=MGA3 / ATCC 53907;
RX PubMed=30119014; DOI=10.1016/j.jinorgbio.2018.08.002;
RA Girvan H.M., Poddar H., McLean K.J., Nelson D.R., Hollywood K.A.,
RA Levy C.W., Leys D., Munro A.W.;
RT "Structural and catalytic properties of the peroxygenase P450 enzyme
RT CYP152K6 from Bacillus methanolicus.";
RL J. Inorg. Biochem. 188:18-28(2018).
CC -!- FUNCTION: Fatty-acid peroxygenase that catalyzes the hydroxylation of
CC dodecanoate with formation of 2-hydroxydodecanoate and only trace
CC amounts of 3-hydroxydodecanoate. Cannot use hexadecanoate as substrate,
CC and from tetradecanoate, forms only a small amount of the 2-
CC hydroxylated form, with large amounts of substrate remaining. Can
CC further convert 2-hydroxydodecanoate into 2,3-dihydroxydodecanoate and
CC 2-hydroxydodec-2-enoate, the latter product likely leads to undec-1-en-
CC 1-ol via oxidative decarboxylation. Thus, this enzyme seems capable of
CC both desaturation and decarboxylation reactions in addition to
CC hydroxylation reactions. {ECO:0000269|PubMed:30119014}.
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:30119014};
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:30119014};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + H2O2 = 2-hydroxydodecanoate + H2O;
CC Xref=Rhea:RHEA:57476, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:141772;
CC Evidence={ECO:0000269|PubMed:30119014};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxydodecanoate + H2O2 = 2,3-dihydroxydodecanoate + H2O;
CC Xref=Rhea:RHEA:57480, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:141772, ChEBI:CHEBI:141780;
CC Evidence={ECO:0000269|PubMed:30119014};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:30119014};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:30119014}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; CP007739; AIE59747.1; -; Genomic_DNA.
DR RefSeq; WP_003349199.1; NZ_CP007739.1.
DR PDB; 6FYJ; X-ray; 1.30 A; A=1-419.
DR PDBsum; 6FYJ; -.
DR AlphaFoldDB; I3DZK9; -.
DR SMR; I3DZK9; -.
DR STRING; 796606.BMMGA3_06595; -.
DR EnsemblBacteria; AIE59747; AIE59747; BMMGA3_06595.
DR KEGG; bmet:BMMGA3_06595; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_037319_0_0_9; -.
DR OrthoDB; 520970at2; -.
DR Proteomes; UP000027602; 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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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; Fatty acid metabolism; Heme; Iron; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome.
FT CHAIN 1..419
FT /note="Fatty-acid peroxygenase"
FT /id="PRO_0000445581"
FT BINDING 61
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:30119014"
FT BINDING 68
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:30119014"
FT BINDING 94
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:30119014"
FT BINDING 98
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:30119014"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30119014"
FT BINDING 365
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:30119014"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:6FYJ"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:6FYJ"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:6FYJ"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6FYJ"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6FYJ"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 107..129
FT /evidence="ECO:0007829|PDB:6FYJ"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 158..173
FT /evidence="ECO:0007829|PDB:6FYJ"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 179..204
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 232..262
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:6FYJ"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:6FYJ"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6FYJ"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6FYJ"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:6FYJ"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:6FYJ"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:6FYJ"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:6FYJ"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:6FYJ"
FT HELIX 368..384
FT /evidence="ECO:0007829|PDB:6FYJ"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:6FYJ"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6FYJ"
FT STRAND 411..417
FT /evidence="ECO:0007829|PDB:6FYJ"
SQ SEQUENCE 419 AA; 48794 MW; 1B894C5F69FB17A9 CRC64;
MSNINQMPRE EGIDSTWRLM EEGYMYILNR RHSFNSDIFE TRLLGKKAIC MGGKEAAEIF
YDTEKFKRKD AAPNRVVQTL FGKNGVQALD GQTHKHRKEM FMSIMSPDEL EKLTDITKKQ
WEIAVDKWEQ MDKVILYEEA KEIMCRTACQ WAGVPVQENE VKRLTKNLGA MFESAAAVGL
KHWLGRHARN YEEIWIEELI DRVRDGKVNP PENTTLHKFS WYRDLEGNLL DTETAAVEVI
NILRPIVAIA IFINFIALAL HHYPEEKEKL KSGDKKYSQM FVQEVRRFYP FFPFVVALVK
KDFTWKGYKF EEGTLTLLDL YGTNHDPEIW KNPDVFSPDR FAKWEGSPFS FIPQGGGDYF
MGHRCAGEWV TIEVMKVSLD YLTNRMDYEV PDQDLSFSMA SMPSIPHSKV VIKNVKKRI
