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C71AJ_APIGR
ID   C71AJ_APIGR             Reviewed;         476 AA.
AC   C0SJS4;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Psoralen synthase;
DE            EC=1.14.14.141 {ECO:0000269|PubMed:19098286};
DE   AltName: Full=Cytochrome P450 CYP71AJ2;
DE   Flags: Fragment;
GN   Name=CYP71AJ2;
OS   Apium graveolens (Celery).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Apium.
OX   NCBI_TaxID=4045;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19098286; DOI=10.1074/jbc.m807351200;
RA   Larbat R., Hehn A., Hans J., Schneider S., Jugde H., Schneider B.,
RA   Matern U., Bourgaud F.;
RT   "Isolation and functional characterization of CYP71AJ4 encoding for the
RT   first P450 monooxygenase of angular furanocoumarin biosynthesis.";
RL   J. Biol. Chem. 284:4776-4785(2009).
CC   -!- FUNCTION: Involved in linear furanocumarin (psoralen) biosynthesis.
CC       Converts marmesin to psoralen and, with much lower affinity, 5-
CC       hydroxymarmesin to bergaptol. {ECO:0000269|PubMed:19098286}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7S)-marmesin + O2 + reduced [NADPH--hemoprotein reductase] =
CC         acetone + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] +
CC         psoralen; Xref=Rhea:RHEA:19281, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:6695, ChEBI:CHEBI:15347, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:27616,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.141;
CC         Evidence={ECO:0000269|PubMed:19098286};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.54 uM for marmesin {ECO:0000269|PubMed:19098286};
CC         KM=54 uM for 5-hydroxymarmesin {ECO:0000269|PubMed:19098286};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:19098286};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- BIOTECHNOLOGY: Psoralen possesses photocarcinogen properties. It
CC       intercalates in double-stranded DNA and cross-links pyrimidine bases
CC       under UV-A irradiation. Psoralen is widely used in combination with UV-
CC       A radiation to treat a variety of skin disorders like psoriasis or
CC       eczema.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; EF191022; ABO84855.1; -; mRNA.
DR   AlphaFoldDB; C0SJS4; -.
DR   SMR; C0SJS4; -.
DR   BRENDA; 1.14.14.141; 388.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0102876; F:psoralen synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           <1..>476
FT                   /note="Psoralen synthase"
FT                   /id="PRO_0000401482"
FT   TRANSMEM        1..18
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         476
SQ   SEQUENCE   476 AA;  53543 MW;  D7C544517721A8AF CRC64;
     YFFSLFLVTV FVYKLLTLKK TPSKNLPPSP PRYPIIGNLH QIGPDPQHSL RDLALKYGPL
     MSLKFGTVPV LVVSSADAAR EVLKTHDLIF ADRPYSSVAN KVFYNGKDMV FARYTEYWRQ
     VKSICVTQLL SNKRVNSFQN VREEEVDLLV QNIENSCSKV INLTELLIEV TGNVVCKVSV
     GSGDKVDSYK ILILEIMEML GYSRSIEDFF PMFGWVDWLT GLRGKVAKAA KGVDDFLEGV
     LKEHLTARAS NNASADNDFV SILLEIQEAD AGSTMDNECI KSLIWDMLGA GTETISTALE
     WTLAALIKNP DAMLKLQNEV REIGKGKSKI SEADLGKMTY LQAVMKESMR LYFTAPLLVP
     RESRQDVKFM GYDISAGTQV LINVWAIARD PSLWEKPEEF RPERFLNSHI DYKGFNYEYL
     PFGAGRRGCP GIQFAMAVNE LVVANVIHKF NFELPDGERL EDLDMTAVSG ITLRKK
 
 
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