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UBIX_AERPE
ID   UBIX_AERPE              Reviewed;         197 AA.
AC   Q9YBF0;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Flavin prenyltransferase UbiX {ECO:0000255|HAMAP-Rule:MF_01984};
DE            EC=2.5.1.129 {ECO:0000255|HAMAP-Rule:MF_01984};
GN   Name=ubiX {ECO:0000255|HAMAP-Rule:MF_01984}; OrderedLocusNames=APE_1647;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- FUNCTION: Flavin prenyltransferase that catalyzes the synthesis of the
CC       prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic
CC       acid decarboxylase UbiD. The prenyltransferase is metal-independent and
CC       links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to
CC       the flavin N5 and C6 atoms of FMN. {ECO:0000255|HAMAP-Rule:MF_01984}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2;
CC         Xref=Rhea:RHEA:37743, ChEBI:CHEBI:43474, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:87467, ChEBI:CHEBI:88052; EC=2.5.1.129;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01984};
CC   -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01984}.
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DR   EMBL; BA000002; BAA80648.1; -; Genomic_DNA.
DR   PIR; C72545; C72545.
DR   AlphaFoldDB; Q9YBF0; -.
DR   SMR; Q9YBF0; -.
DR   STRING; 272557.APE_1647; -.
DR   EnsemblBacteria; BAA80648; BAA80648; APE_1647.
DR   KEGG; ape:APE_1647; -.
DR   eggNOG; arCOG01703; Archaea.
DR   OMA; GATHIQD; -.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1950; -; 1.
DR   HAMAP; MF_01984; ubiX_pad; 1.
DR   InterPro; IPR036551; Flavin_trans-like.
DR   InterPro; IPR003382; Flavoprotein.
DR   InterPro; IPR004507; UbiX-like.
DR   PANTHER; PTHR43374; PTHR43374; 1.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF52507; SSF52507; 1.
DR   TIGRFAMs; TIGR00421; ubiX_pad; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Prenyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..197
FT                   /note="Flavin prenyltransferase UbiX"
FT                   /id="PRO_0000134976"
FT   BINDING         14..16
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         40
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         94..97
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         129
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         159
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         175
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
SQ   SEQUENCE   197 AA;  21185 MW;  BB878C6DB14C4B7F CRC64;
     MSCRPSSVSI AVTGSSGVRV ALRLLEALKG EVEIRGIILT RGAEEVARYE EGIEPEDLRR
     LLRSYAPLYM ENDMSSPLAS SSNQPDAMAI VPASMKTVGL IARGIPSSLP ARAALAVLRL
     GRRLVVAPRE TPLGVVELEN MLAIARMGGI VVPLTLSFYI KPSSVEDLVD FAAGKVLDAL
     GVKVDVYRRW RGPEEGD
 
 
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