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Database: UniProt
Entry: A0A0F7IEP8_9EURY
LinkDB: A0A0F7IEP8_9EURY
Original site: A0A0F7IEP8_9EURY 
ID   A0A0F7IEP8_9EURY        Unreviewed;       182 AA.
AC   A0A0F7IEP8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Flavin prenyltransferase UbiX {ECO:0000256|HAMAP-Rule:MF_01984};
DE            EC=2.5.1.129 {ECO:0000256|HAMAP-Rule:MF_01984};
GN   Name=ubiX {ECO:0000256|HAMAP-Rule:MF_01984};
GN   ORFNames=GAH_01570 {ECO:0000313|EMBL:AKG91142.1};
OS   Geoglobus ahangari.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Geoglobus.
OX   NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG91142.1, ECO:0000313|Proteomes:UP000034723};
RN   [1] {ECO:0000313|EMBL:AKG91142.1, ECO:0000313|Proteomes:UP000034723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=234 {ECO:0000313|EMBL:AKG91142.1,
RC   ECO:0000313|Proteomes:UP000034723};
RA   Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA   Kashefi K.;
RT   "The complete genome sequence of the hyperthermophilic, obligate iron-
RT   reducing archaeon Geoglobus ahangari strain 234T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01984};
CC   -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01984}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01984}.
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DR   EMBL; CP011267; AKG91142.1; -; Genomic_DNA.
DR   RefSeq; WP_048095932.1; NZ_CP011267.1.
DR   AlphaFoldDB; A0A0F7IEP8; -.
DR   STRING; 113653.GAH_01570; -.
DR   GeneID; 24804139; -.
DR   KEGG; gah:GAH_01570; -.
DR   PATRIC; fig|113653.22.peg.1548; -.
DR   HOGENOM; CLU_074522_0_1_2; -.
DR   InParanoid; A0A0F7IEP8; -.
DR   OrthoDB; 9540at2157; -.
DR   Proteomes; UP000034723; Chromosome.
DR   GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1950; Flavin prenyltransferase-like; 1.
DR   HAMAP; MF_01984; ubiX_pad; 1.
DR   InterPro; IPR036551; Flavin_trans-like.
DR   InterPro; IPR003382; Flavoprotein.
DR   InterPro; IPR004507; UbiX-like.
DR   NCBIfam; TIGR00421; ubiX_pad; 1.
DR   PANTHER; PTHR43374; FLAVIN PRENYLTRANSFERASE; 1.
DR   PANTHER; PTHR43374:SF1; FLAVIN PRENYLTRANSFERASE PAD1, MITOCHONDRIAL; 1.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF52507; Homo-oligomeric flavin-containing Cys decarboxylases, HFCD; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01984};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01984};
KW   Lyase {ECO:0000313|EMBL:AKG91142.1};
KW   Prenyltransferase {ECO:0000256|ARBA:ARBA00022602, ECO:0000256|HAMAP-
KW   Rule:MF_01984}; Reference proteome {ECO:0000313|Proteomes:UP000034723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01984}.
FT   DOMAIN          1..163
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   BINDING         9..11
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         35
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         86..89
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         121
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         151
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         167
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
SQ   SEQUENCE   182 AA;  20138 MW;  D885C8B0C1A2F939 CRC64;
     MRYVLAMTGA SGQIFGVRLL EILSENGAEV HLVVSKAAEI TMEHELGKSV EDLEGHAYRV
     YSENDISAGL ASGTFRHDGM AVVPCSVKTL SSIAYGIADN LIVRAADVTL KERRRLVLAV
     RETPLHINHI RAMLRVSQAG AIVMPPVPAF YIHPEKIEDI VDHFAFRVAE VLGMSVDYRR
     WK
//
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