UBIX_SALTY
ID UBIX_SALTY Reviewed; 189 AA.
AC P0A245; P40787;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=STM2356;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-189.
RC STRAIN=ST314;
RX PubMed=7041112; DOI=10.1073/pnas.79.4.1083;
RA Higgins C.F., Ames G.F.-L.;
RT "Regulatory regions of two transport operons under nitrogen control:
RT nucleotide sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1083-1087(1982).
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 -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000255|HAMAP-
CC Rule:MF_01984}.
CC -!- SEQUENCE CAUTION:
CC Sequence=J01798; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=J01798; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL21257.1; -; Genomic_DNA.
DR EMBL; J01798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_461298.1; NC_003197.2.
DR RefSeq; WP_000825682.1; NC_003197.2.
DR AlphaFoldDB; P0A245; -.
DR SMR; P0A245; -.
DR STRING; 99287.STM2356; -.
DR PaxDb; P0A245; -.
DR EnsemblBacteria; AAL21257; AAL21257; STM2356.
DR GeneID; 1253878; -.
DR KEGG; stm:STM2356; -.
DR PATRIC; fig|99287.12.peg.2494; -.
DR HOGENOM; CLU_074522_0_1_6; -.
DR OMA; GATHIQD; -.
DR PhylomeDB; P0A245; -.
DR BioCyc; SENT99287:STM2356-MON; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway.
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..189
FT /note="Flavin prenyltransferase UbiX"
FT /id="PRO_0000134953"
FT BINDING 10..12
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 88..91
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 189 AA; 20691 MW; 2274B1935D10E649 CRC64;
MKRLIVGISG ASGAIYGVRL LQILRDVDSV ETHLVMSQAA RQTLALETHF SLREVQALAD
VTHDARDIAA SISSGSYPTA GMVILPCSIK TLSGIVHSYT DGLLTRAADV ILKERRPLVL
CVRETPLHIG HLRLMTQAAE IGAVIMPPVP AFYHLPQTLD DVINQTVNRV LDQFDIPLPH
DLFVRWQGA
