ID   UBIX_SYNY3              Reviewed;         206 AA.
AC   P72743;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=slr1099;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA16758.1; -; Genomic_DNA.
DR   PIR; S74606; S74606.
DR   AlphaFoldDB; P72743; -.
DR   SMR; P72743; -.
DR   STRING; 1148.1651831; -.
DR   PaxDb; P72743; -.
DR   EnsemblBacteria; BAA16758; BAA16758; BAA16758.
DR   KEGG; syn:slr1099; -.
DR   eggNOG; COG0163; Bacteria.
DR   InParanoid; P72743; -.
DR   OMA; GATHIQD; -.
DR   PhylomeDB; P72743; -.
DR   BioCyc; MetaCyc:MON-18477; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..206
FT                   /note="Flavin prenyltransferase UbiX"
FT                   /id="PRO_0000134973"
FT   BINDING         11..13
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         37
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         103..106
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         138
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         168
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         184
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
SQ   SEQUENCE   206 AA;  22173 MW;  7C1E13F479996E3F CRC64;
     MAQPLILGVS GASGLIYAVR AIKHLLAADY TIELVASRAS YQVWQAEQNI QMPGEPSAQA
     EFWRSQAGVE KGGKLICHRW GDVGATIASG SYRCAGMVVL PCSMSTVAKL AVGMSSDLLE
     RAADVQIKEG KPLVVVPRET PLSLIHLRNL TSLAEAGVRI VPAIPAWYHQ PQSVEDLVDF
     VVARALDQLA IDCVPLQRWQ GGMEGE