CYP28_STRAW
ID CYP28_STRAW Reviewed; 402 AA.
AC Q825I8;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Pentalenic acid synthase;
DE EC=1.14.15.11;
GN Name=cyp28; Synonyms=cyp105d7; OrderedLocusNames=SAV_7469;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [3]
RP PATHWAY.
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=21250661; DOI=10.1021/bi1019786;
RA Seo M.J., Zhu D., Endo S., Ikeda H., Cane D.E.;
RT "Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger
RT monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the
RT final steps of the biosynthesis of pentalenolactone and
RT neopentalenolactone.";
RL Biochemistry 50:1739-1754(2011).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=21081950; DOI=10.1038/ja.2010.135;
RA Takamatsu S., Xu L.H., Fushinobu S., Shoun H., Komatsu M., Cane D.E.,
RA Ikeda H.;
RT "Pentalenic acid is a shunt metabolite in the biosynthesis of the
RT pentalenolactone family of metabolites: hydroxylation of 1-deoxypentalenic
RT acid mediated by CYP105D7 (SAV_7469) of Streptomyces avermitilis.";
RL J. Antibiot. 64:65-71(2011).
CC -!- FUNCTION: Catalyzes the conversion of 1-deoxypentalenic acid to
CC pentalenic acid in the biosynthesis of neopentalenolactone antibiotic.
CC {ECO:0000269|PubMed:21081950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-deoxypentalenate + 2 H(+) + O2 + reduced 2[4Fe-4S]-
CC [ferredoxin] = H2O + oxidized 2[4Fe-4S]-[ferredoxin] + pentalenate;
CC Xref=Rhea:RHEA:34499, Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33722, ChEBI:CHEBI:33723, ChEBI:CHEBI:68649,
CC ChEBI:CHEBI:68650; EC=1.14.15.11;
CC Evidence={ECO:0000269|PubMed:21081950};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Antibiotic biosynthesis; neopentalenolactone biosynthesis.
CC {ECO:0000269|PubMed:21250661}.
CC -!- MISCELLANEOUS: S.avermitilis does not produce pentalenolactone itself
CC in vivo but instead a group of new metabolites that are
CC neopentalenolactone derivatives. {ECO:0000305|PubMed:21250661}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; BA000030; BAC75180.2; -; Genomic_DNA.
DR PDB; 4UBS; X-ray; 2.20 A; A=10-402.
DR PDBsum; 4UBS; -.
DR AlphaFoldDB; Q825I8; -.
DR SMR; Q825I8; -.
DR STRING; 227882.SAV_7469; -.
DR EnsemblBacteria; BAC75180; BAC75180; SAVERM_7469.
DR KEGG; sma:SAVERM_7469; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_1_1_11; -.
DR OMA; WHRPARH; -.
DR OrthoDB; 816674at2; -.
DR BioCyc; MetaCyc:MONMETA-16855; -.
DR BRENDA; 1.14.15.11; 5980.
DR UniPathway; UPA01021; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016713; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR GO; GO:1901336; P:lactone biosynthetic process; IDA:UniProtKB.
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 3D-structure; Antibiotic biosynthesis; Heme; Iron; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..402
FT /note="Pentalenic acid synthase"
FT /id="PRO_0000422009"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 351
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"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:4UBS"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:4UBS"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:4UBS"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 113..137
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:4UBS"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 183..206
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 228..258
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 274..285
FT /evidence="ECO:0007829|PDB:4UBS"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:4UBS"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4UBS"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:4UBS"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:4UBS"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:4UBS"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:4UBS"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 354..371
FT /evidence="ECO:0007829|PDB:4UBS"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:4UBS"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:4UBS"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:4UBS"
SQ SEQUENCE 402 AA; 44113 MW; 224CDCFB08FC2153 CRC64;
MTEPGTSVSA PVAFPQDRTC PYDPPTAYDP LREGRPLSRV SLYDGRSVWV VTGHAAARAL
LSDQRLSSDR TLPRFPATTE RFEAVRTRRV ALLGVDDPEH RTQRRMLVPS FTLKRAAALR
PRIQETVDGL LDAMEAQGPP AELVSAFALP LPSMVICALL GVPYADHDFF ESQSRRLLRG
PGIAEVQDAR AQLDDYLYAL IDRKRKEPGD GLLDDLIQEQ LNRGTVDRAE LVSLATLLLI
AGHETTANMI SLGTFTLLRH PEQLAELRAE PGLMPAAVEE LLRFLSIADG LLRVATEDIE
VAGTTIRADE GVVFATSVIN RDAAGFAEPD ALDWHRSARH HVAFGFGIHQ CLGQNLARAE
MEIALGTLFE RLPGLRLAAP ADEIPFKPGD TIQGMLELPV TW
