UBIX_THEAC
ID UBIX_THEAC Reviewed; 180 AA.
AC Q9HJ72;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Ta1100;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445066; CAC12227.1; -; Genomic_DNA.
DR RefSeq; WP_010901510.1; NC_002578.1.
DR AlphaFoldDB; Q9HJ72; -.
DR SMR; Q9HJ72; -.
DR STRING; 273075.Ta1100; -.
DR EnsemblBacteria; CAC12227; CAC12227; CAC12227.
DR GeneID; 1456609; -.
DR KEGG; tac:Ta1100; -.
DR eggNOG; arCOG01703; Archaea.
DR HOGENOM; CLU_074522_2_1_2; -.
DR OMA; GATHIQD; -.
DR OrthoDB; 112962at2157; -.
DR Proteomes; UP000001024; 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..180
FT /note="Flavin prenyltransferase UbiX"
FT /id="PRO_0000134983"
FT BINDING 9..11
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 33
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 84..87
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 119
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 149
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 165
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
SQ SEQUENCE 180 AA; 19774 MW; 4E2A2ADC972EB229 CRC64;
MRIVVGISGA SGIPYAVRFL ENLRGHDTYL VISEAAKKVI QYESDENIEY IRSLASHNYE
DDDFSAPISS GSFLFDSMVI VPCSITTISK IAAGISDTLI TRAAAVSLKE RRRLIVVPRE
MPLSTIDLKN MTYLSENGVI VAPASPGFYT KPKSVDDMVA FVVSRILDLV GVGNDLIKRW