ID   YL894_MIMIV             Reviewed;         438 AA.
AC   Q5UQZ1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Putative truncated GMC-type inactive oxidoreductase L894;
DE   Flags: Precursor;
GN   OrderedLocusNames=MIMI_L894;
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 [LARGE SCALE 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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16971431}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
CC   -!- CAUTION: The two ORFs L894 and L893 correspond respectively to the
CC       N- and C-terminal of a GMC-type oxidoreductase. {ECO:0000305}.
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DR   EMBL; AY653733; AAV51151.1; -; Genomic_DNA.
DR   SMR; Q5UQZ1; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   PANTHER; PTHR11552; PTHR11552; 1.
DR   Pfam; PF00732; GMC_oxred_N; 2.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Reference proteome; Signal; Virion.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..438
FT                   /note="Putative truncated GMC-type inactive oxidoreductase
FT                   L894"
FT                   /id="PRO_0000243957"
FT   BINDING         79..109
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   438 AA;  48304 MW;  9F693A7E6BEC45AD CRC64;
     MYVFLLFSRY KIFYVYIKKM AHRSRCNCND TSNSNGSQHG INLPLRKIDT YDPCVNCRVK
     PHLCPKPHPC PKPENLEADI VIIGAGAAGC VLAYYLTKFS DLKIILLEAG HTHFNDPVVT
     DPMGFFGKYN PPNENIRMSQ NPSYAWQPAL EPDTGAYSMR NVVAHGLAVG GSTAINQLNY
     IVGGRTVFDN DWPTGWKYDD IKKYFRRVLA DISPIRDGTK VNLTNTILES MRVLADQQVS
     SGVPVDFLIN KATGGLPNIE QTYQGAPIVN LNDYEGINSV CGFKSYYVGV NQLSDGSYIR
     KYAGNTYLNS YYVDSNGFGI GKFSNLRVIS DAVVDRIHFE GQRAVSVTYI DKKGNLHSVK
     VHKEVEICSG SFFTPTILQR SGIGDFSYLS SIGVPDLVYN NPLVGQGLRN HYSPITQVSV
     TGPDAAAFLS NTAAGPTI