ID   YL532_MIMIV             Reviewed;         468 AA.
AC   Q5UQ90;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Cytochrome P450-like protein L532;
DE            EC=1.14.14.-;
GN   OrderedLocusNames=MIMI_L532;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA   Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA   Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT   "Mimivirus giant particles incorporate a large fraction of anonymous and
RT   unique gene products.";
RL   J. Virol. 80:11678-11685(2006).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Virion {ECO:0000269|PubMed:16971431}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50796.1; -; Genomic_DNA.
DR   SMR; Q5UQ90; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0033644; C:host cell 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; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   1: Evidence at protein level;
KW   Heme; Host membrane; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW   Virion.
FT   CHAIN           1..468
FT                   /note="Cytochrome P450-like protein L532"
FT                   /id="PRO_0000253240"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         415
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   468 AA;  54115 MW;  86D2E2A988BF662B CRC64;
     MVLSDILFSI YEHREKSPVF SWFAYLLRIL DWIIQFLSFG LIPSIGGDLY DLVDNGLFKF
     VLDRNIQKKQ NQLYDKFRLG TVKMCLVFDG ELTKKLLLDN SIRRGGLYNL LTKFFGKGIF
     TSNIHSRWMK QRKAIFKLFS PQNLIQITPE LTTSMFEELD RLITIKKDLD LVTVLSLIGL
     VGFCKVIFGV DVTDMSEELI EPLNDLLIYI NGAVEPVLIT ADPSYRRFIT NKKFVHNWMR
     KLIDKARKSE NCFEIMRQQL DDIGSDDETE LIEFILSVVL GGHETTARLM LGIIYSVCHN
     KEIIEKLNNE TDEYPKGDYI NLKKRPYLNN IIKEGTRLFP PVWLLSREAK NDTTIDNHFF
     KKGTQFLISP LIILRDYNVW GSNAEKFDPE RFSNMDPKSK ASKLYIPFIV GSEDCPGKKF
     AILESAIVVS KLFKEYEITV LKHKLNPMSA GTFRLSDKLP VSIKKLKN