CP107_PRIM1
ID CP107_PRIM1 Reviewed; 410 AA.
AC D5E3H2;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Cytochrome P450 CYP107DY1 {ECO:0000303|PubMed:27816653};
DE EC=1.14.-.- {ECO:0000269|PubMed:27816653};
DE AltName: Full=Mevastatin hydroxylase {ECO:0000305|PubMed:27816653};
GN OrderedLocusNames=BMQ_pBM50008 {ECO:0000312|EMBL:ADE72347.1};
OS Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium).
OG Plasmid pBM500 {ECO:0000312|EMBL:ADE72347.1,
OG ECO:0000312|Proteomes:UP000000935}.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=545693;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12872 / QMB1551;
RX PubMed=21705586; DOI=10.1128/jb.00449-11;
RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA Bremer E., Jahn D., Ravel J., Vary P.S.;
RT "Genome sequences of the biotechnologically important Bacillus megaterium
RT strains QM B1551 and DSM319.";
RL J. Bacteriol. 193:4199-4213(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, 3D-STRUCTURE MODELING, AND
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 12872 / QMB1551;
RX PubMed=27816653; DOI=10.1016/j.jbiotec.2016.11.002;
RA Milhim M., Putkaradze N., Abdulmughni A., Kern F., Hartz P., Bernhardt R.;
RT "Identification of a new plasmid-encoded cytochrome P450 CYP107DY1 from
RT Bacillus megaterium with a catalytic activity towards mevastatin.";
RL J. Biotechnol. 240:68-75(2016).
CC -!- FUNCTION: Cytochrome P450 whose physiological substrate is unknown. In
CC vitro, is able to catalyze the selective hydroxylation of mevastatin to
CC pravastatin, the widely used therapeutic agent for
CC hypercholesterolemia. {ECO:0000269|PubMed:27816653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + mevastatin + O2 + 2 reduced [2Fe-2S]-[ferredoxin] =
CC H2O + 2 oxidized [2Fe-2S]-[ferredoxin] + pravastatin lactone;
CC Xref=Rhea:RHEA:51668, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:34848,
CC ChEBI:CHEBI:145933; Evidence={ECO:0000269|PubMed:27816653};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:27816653};
CC -!- BIOTECHNOLOGY: Could be a valuable biocatalyst used in the industrial
CC field for an efficient biotransformation of mevastatin.
CC {ECO:0000305|PubMed:27816653}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; CP001988; ADE72347.1; -; Genomic_DNA.
DR RefSeq; WP_013060111.1; NC_014025.1.
DR AlphaFoldDB; D5E3H2; -.
DR SMR; D5E3H2; -.
DR EnsemblBacteria; ADE72347; ADE72347; BMQ_pBM50008.
DR KEGG; bmq:BMQ_pBM50008; -.
DR HOGENOM; CLU_033716_1_0_9; -.
DR OMA; NCIFLLN; -.
DR OrthoDB; 816674at2; -.
DR Proteomes; UP000000935; Plasmid pBM500.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
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 Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase; Plasmid;
KW Reference proteome.
FT CHAIN 1..410
FT /note="Cytochrome P450 CYP107DY1"
FT /id="PRO_0000439192"
FT BINDING 106
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:Q59523"
FT BINDING 110
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:Q59523"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27816653"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27816653"
FT BINDING 302
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:Q59523"
FT BINDING 358
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:Q59523"
FT BINDING 360
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:0000250|UniProtKB:Q59523"
SQ SEQUENCE 410 AA; 46742 MW; 423298DFBA326CA2 CRC64;
MKKVTVDDFS SPENMHDVIG FYKKLTEHQE PLIRLDDYYG LGPAWVALRH DDVVTILKNP
RFLKDVRKFT PLQDKKDSID DSTSASKLFE WMMNMPNMLT VDPPDHTRLR RLASKAFTPR
MIENLRPRIQ QITNELLDSV EGKRNMDLVA DFSFPLPIIV ISEMLGIPPL DQKRFRDWTD
KLIKAAMDPS QGAVVMETLK EFIDYIKKML VEKRNHPDDD VMSALLQAHE QEDKLSENEL
LSTIWLLITA GHETTAHLIS NGVLALLKHP EQMRLLRDNP SLLPSAVEEL LRYAGPVMIG
GRFAGEDIIM HGKMIPKGEM VLFSLVAANI DSQKFSYPEG LDITREENEH LTFGKGIHHC
LGAPLARMEA HIAFGTLLQR FPDLRLAIES EQLVYNNSTL RSLKSLPVIF
