ID   CPS2_STRCC              Reviewed;         410 AA.
AC   Q59831;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Cytochrome P450 105A3;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450 sca-2;
DE            Short=CYT P-450sca-2;
GN   Name=cyp105A3;
OS   Streptomyces carbophilus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=44059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=SANK 62585;
RX   PubMed=7557483; DOI=10.1016/0378-1119(95)00394-l;
RA   Watanabe I., Nara F., Serizawa N.;
RT   "Cloning, characterization and expression of the gene encoding cytochrome
RT   P-450sca-2 from Streptomyces carbophilus involved in production of
RT   pravastatin, a specific HMG-CoA reductase inhibitor.";
RL   Gene 163:81-85(1995).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=2509201; DOI=10.1111/j.1432-1033.1989.tb15070.x;
RA   Matsuoka T., Miyakoshi S., Tanzawa K., Nakahara K., Hosobuchi M.,
RA   Serizawa N.;
RT   "Purification and characterization of cytochrome P-450sca from Streptomyces
RT   carbophilus. ML-236B (compactin) induces a cytochrome P-450sca in
RT   Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium
RT   (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-
RT   coenzyme-A reductase.";
RL   Eur. J. Biochem. 184:707-713(1989).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=10329788; DOI=10.1107/s0907444999003716;
RA   Ito S., Matsuoka T., Watanabe I., Kagasaki T., Serizawa N., Hata T.;
RT   "Crystallization and preliminary X-ray diffraction analysis of cytochrome
RT   P450sca-2 from Streptomyces carbophilus involved in production of
RT   pravastatin sodium, a tissue-selective inhibitor of HMG-CoA reductase.";
RL   Acta Crystallogr. D 55:1209-1211(1999).
CC   -!- FUNCTION: Catalyzes the hydroxylation of sodium ML-236B carboxylate to
CC       pravastatin. {ECO:0000269|PubMed:2509201}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer.
CC   -!- INDUCTION: By sodium ML-236B carboxylate. {ECO:0000269|PubMed:2509201}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D30815; BAA06492.1; -; Genomic_DNA.
DR   PIR; JC4287; JC4287.
DR   AlphaFoldDB; Q59831; -.
DR   SMR; Q59831; -.
DR   PRIDE; Q59831; -.
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; 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   Direct protein sequencing; Heme; Iron; Metal-binding; Monooxygenase;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7557483"
FT   CHAIN           2..410
FT                   /note="Cytochrome P450 105A3"
FT                   /id="PRO_0000052214"
FT   BINDING         359
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"
SQ   SEQUENCE   410 AA;  45049 MW;  23E8735606942264 CRC64;
     MTEMTEKATT FLTSQEAPAF PADRTCPYQL PTAYSRLRDE PDALRPVTLY DGRRAWVVTK
     HEAARRLLAD PRLSSDRLHA DFPATSPRFK AFRQGSPAFI GMDPPEHGTR RRMTISEFTV
     KRIKGMRPDV ERIVHGFIDD MLAAGPTADL VSQFALPVPS MVICHMLGVP YADHEFFQDA
     SKRLVQAVDA DSAVAARDDF ERYLDGLITK LESEPGTGLL GKLVTHQLAD GEIDRAELIS
     TALLLLVAGH ETTASMTSLS VITLLEHPDQ HAALRADPSL VPGAVEELLR VLAIADIAGG
     RIATADIEID GQLIRAGEGV IVTNSIANRD SSVFENPDRL DVHRSARHHL SFGYGVHQCL
     GQNLARLELE VILTVLFDRI PTLRLAVPVE QLTLRPGTTI QGVNELPVTW