CPXK_SACEN
ID CPXK_SACEN Reviewed; 405 AA.
AC P33271; A4FLS3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cytochrome P450 107B1;
DE EC=1.14.-.-;
DE AltName: Full=Cytochrome P450CVIIB1;
GN Name=cyp107B1; Synonyms=cypA; OrderedLocusNames=SACE_5814;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 172-203 AND
RP 302-321.
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=1732208; DOI=10.1128/jb.174.3.725-735.1992;
RA Andersen J.F., Hutchinson C.R.;
RT "Characterization of Saccharopolyspora erythraea cytochrome P-450 genes and
RT enzymes, including 6-deoxyerythronolide B hydroxylase.";
RL J. Bacteriol. 174:725-735(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
CC -!- FUNCTION: Not known, probably involved in the catabolism of octane and
CC guaiacol. It displays a weak activity in the O-dealkylation of 7-
CC ethoxycoumarin.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M83110; AAA26483.1; -; Genomic_DNA.
DR EMBL; AM420293; CAM04998.1; -; Genomic_DNA.
DR PIR; B42606; B42606.
DR RefSeq; WP_009943182.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; P33271; -.
DR SMR; P33271; -.
DR STRING; 405948.SACE_5814; -.
DR EnsemblBacteria; CAM04998; CAM04998; SACE_5814.
DR KEGG; sen:SACE_5814; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_1_0_11; -.
DR OMA; PICMATT; -.
DR OrthoDB; 816674at2; -.
DR Proteomes; UP000006728; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Cytoplasm; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..405
FT /note="Cytochrome P450 107B1"
FT /id="PRO_0000052221"
FT BINDING 352
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 405 AA; 45238 MW; 71C93CEC1FDC53FD CRC64;
MTTGEVPDLL AFDDAFAQDR HNRYARMREE PVQRIRTVNG LDAWLITRYE DVKQALLDPR
IAKDFGRTQQ IIEKRLADAE RRPGFSPDLG PHMLNTDPPD HTRLRKLVVK AFTARRVEGL
RPRIEQITDD LLDRLAGRSE VDLIDEFAFP LPITVISELM GVEDSRRDDF RSWTNVLVDG
SQPEAQAQAS VAMVEYLTEL IAKKRTEPGD DLLTALLEAV EDGDRLSEGE LIAMVFLLLV
AGHETTVNLI GNCVLSLLGN PDQLAALRND PSLLPGAIEE TLRYESPVAN GTFRHTAEAV
RFGDVVIPEG ELVWVALGAA NRDGERFEDP DRFDITRETT GHVAFGHGIH FCVGAALARL
EAQIAVGRLL ERFPDLRMAA SPDDLRWRFS VLMRGLEKLP VRPGA