ID   UBIX_HELPY              Reviewed;         187 AA.
AC   O26011;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=HP_1476;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000511; AAD08515.1; -; Genomic_DNA.
DR   PIR; D64704; D64704.
DR   RefSeq; NP_208267.1; NC_000915.1.
DR   RefSeq; WP_000780126.1; NC_018939.1.
DR   AlphaFoldDB; O26011; -.
DR   SMR; O26011; -.
DR   STRING; 85962.C694_07640; -.
DR   PaxDb; O26011; -.
DR   EnsemblBacteria; AAD08515; AAD08515; HP_1476.
DR   KEGG; hpy:HP_1476; -.
DR   PATRIC; fig|85962.47.peg.1587; -.
DR   eggNOG; COG0163; Bacteria.
DR   OMA; GATHIQD; -.
DR   PhylomeDB; O26011; -.
DR   BioCyc; MetaCyc:HP_RS07310-MON; -.
DR   Proteomes; UP000000429; 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; 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..187
FT                   /note="Flavin prenyltransferase UbiX"
FT                   /id="PRO_0000134966"
FT   BINDING         9..11
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         34
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         123
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         153
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         169
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
SQ   SEQUENCE   187 AA;  20586 MW;  92E1361FDA49AFB0 CRC64;
     MKLVLGISGA SGIPLALRFL EKLPKEIEVF VVASKNAHVV ALEESNINLK NAMKDLRPSG
     TFFNEQDIHA SIASGSYGIH KMAIIPASMD MVAKIAHGFG GDLISRSASV MLKEKRPLLI
     APREMPLSAI MLENLLKLSH SNAIIAPPMM TYYTQSKTLE AMQDFLVGKW FDSLGIENDL
     YPRWGMN