ID   UBIX_PYRAB              Reviewed;         181 AA.
AC   Q9V030; G8ZID3;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=PYRAB09680;
GN   ORFNames=PAB0651;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248286; CAB49876.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70374.1; -; Genomic_DNA.
DR   PIR; G75071; G75071.
DR   RefSeq; WP_010868085.1; NC_000868.1.
DR   AlphaFoldDB; Q9V030; -.
DR   SMR; Q9V030; -.
DR   STRING; 272844.PAB0651; -.
DR   EnsemblBacteria; CAB49876; CAB49876; PAB0651.
DR   GeneID; 1496318; -.
DR   KEGG; pab:PAB0651; -.
DR   PATRIC; fig|272844.11.peg.1020; -.
DR   eggNOG; arCOG01703; Archaea.
DR   HOGENOM; CLU_074522_0_1_2; -.
DR   OMA; GATHIQD; -.
DR   OrthoDB; 112962at2157; -.
DR   PhylomeDB; Q9V030; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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; 2.
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; Transferase.
FT   CHAIN           1..181
FT                   /note="Flavin prenyltransferase UbiX"
FT                   /id="PRO_0000134980"
FT   BINDING         9..11
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         35
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         79..82
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         114
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         144
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         160
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
SQ   SEQUENCE   181 AA;  19937 MW;  1EB60CBE9BE35A4F CRC64;
     MRVVVAITGA SGTIYGIKLY ETLRDLGHEV ILLASKTGIK VAKYETGIEV KPDFSEDELF
     APIASGSYPF DAMVIAPCSM KTLSAIANGF SNNLITRAAD VALKERRKLV LLIRETPLNL
     IHIQNMLKIT QAGGIIMPAS PAFYHKPGTI DDMIKFIIGK ILDVLGINHN LYKRWGMDYN
     D