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CPXH_STRGR
ID   CPXH_STRGR              Reviewed;         412 AA.
AC   P26911;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cytochrome P450-SOY;
DE            EC=1.14.-.-;
GN   Name=cyp105D1; Synonyms=soyC;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13273 / DSM 12135 / NBRC 3746;
RX   PubMed=1406253; DOI=10.1111/j.1365-2958.1992.tb01386.x;
RA   Trower M.K., Lenstra R., Omer C., Buchholz S.E., Sariaslani F.S.;
RT   "Cloning, nucleotide sequence determination and expression of the genes
RT   encoding cytochrome P-450soy (soyC) and ferredoxinsoy (soyB) from
RT   Streptomyces griseus.";
RL   Mol. Microbiol. 6:2125-2134(1992).
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; X63601; CAA45146.1; -; Genomic_DNA.
DR   PIR; S24750; S24750.
DR   AlphaFoldDB; P26911; -.
DR   SMR; P26911; -.
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; 2.
DR   PRINTS; PR00359; BP450.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..412
FT                   /note="Cytochrome P450-SOY"
FT                   /id="PRO_0000052217"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         361
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   412 AA;  45411 MW;  6843720C9F025AB5 CRC64;
     MTESTTDPAR QNLDPTSPAP ATSFPQDRGC PYHPPAGYAP LREGRPLSRV TLFDGRPVWA
     VTGHALARRL LADPRLSTDR SHPDFPVPAE RFAGAQRRRV ALLGVDDPEH NTQRRMLIPT
     FSVKRIGALR PRIQETVDRL LDAMERQGPP AELVSAFALP VPSMVICALL GVPYADHAFF
     EERSQRLLRG PGADDVNRAR DELEEYLGAL IDRKRAEPGD GLLDELIHRD HPDGPVDREQ
     LVAFAVILLI AGHETTANMI SLGTFTLLSH PEQLAALRAG GTSTAVVVEE LLRFLSIAEG
     LQRLATEDME VDGATIRKGE GVVFSTSLIN RDADVFPRAE TLDWDRPARH HLAFGFGVHQ
     CLGQNLARAE LDIAMRTLFE RLPGLRLAVP AHEIRHKPGD TIQGLLDLPV AW
 
 
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