ID   C94A1_VICSA             Reviewed;         514 AA.
AC   O81117;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cytochrome P450 94A1;
DE            EC=1.14.-.-;
DE   AltName: Full=P450-dependent fatty acid omega-hydroxylase;
GN   Name=CYP94A1; Synonyms=VAGH111;
OS   Vicia sativa (Spring vetch) (Tare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seedling;
RX   PubMed=9601090; DOI=10.1042/bj3320583;
RA   Tijet N., Helvig C., Pinot F., Le Bouquin R., Lesot A., Durst F.,
RA   Salauen J.-P., Benveniste I.;
RT   "Functional expression in yeast and characterization of a clofibrate-
RT   inducible plant cytochrome P-450 (CYP94A1) involved in cutin monomers
RT   synthesis.";
RL   Biochem. J. 332:583-589(1998).
CC   -!- FUNCTION: Catalyzes the omega-hydroxylation of various fatty acids (FA)
CC       from 10 to 18 carbon atoms. The substrate specificity is higher for
CC       laurate > palmitate > myristate > linolenate > linoleate > oleate >
CC       caprate. May play a minor role in cutin synthesis and could be involved
CC       in plant defense.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- INDUCTION: By clofibrate.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF030260; AAD10204.1; -; mRNA.
DR   PIR; T08014; T08014.
DR   AlphaFoldDB; O81117; -.
DR   SMR; O81117; -.
DR   KEGG; ag:AAD10204; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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: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; 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.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..514
FT                   /note="Cytochrome P450 94A1"
FT                   /id="PRO_0000052192"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         458
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   514 AA;  59111 MW;  3D9361380D6C3B0E CRC64;
     MFQFHLEVLL PYLLPLLLLI LPTTIFFLTK PNNKVSSTST NNNIITLPKS YPLIGSYLSF
     RKNLHRRIQW LSDIVQISPS ATFQLDGTLG KRQIITGNPS TVQHILKNQF SNYQKGTTFT
     NTLSDFLGTG IFNTNGPNWK FQRQVASHEF NTKSIRNFVE HIVDTELTNR LIPILTSSTQ
     TNNILDFQDI LQRFTFDNIC NIAFGYDPEY LTPSTNRSKF AEAYEDATEI SSKRFRLPLP
     IIWKIKKYFN IGSEKRLKEA VTEVRSFAKK LVREKKRELE EKSSLETEDM LSRFLSSGHS
     DEDFVADIVI SFILAGKDTT SAALTWFFWL LWKNPRVEEE IVNELSKKSE LMVYDEVKEM
     VYTHAALSES MRLYPPVPMD SKEAVNDDVL PDGWVVKKGT IVTYHVYAMG RMKSLWGDDW
     AEFRPERWLE KDEVNGKWVF VGRDSYSYPV FQAGPRVCLG KEMAFMQMKR IVAGIVGKFK
     VVPEAHLAQE PGFISFLSSQ MEGGFPVTIQ KRDS