UBIX_ECOLI
ID UBIX_ECOLI Reviewed; 189 AA.
AC P0AG03; P09550; P77715;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
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}; Synonyms=dedF;
GN OrderedLocusNames=b2311, JW2308;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3040734; DOI=10.1016/s0021-9258(18)45338-0;
RA Nonet M.L., Marvel C.C., Tolan D.R.;
RT "The hisT-purF region of the Escherichia coli K-12 chromosome.
RT Identification of additional genes of the hisT and purF operons.";
RL J. Biol. Chem. 262:12209-12217(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12799002; DOI=10.1016/s0378-1097(03)00343-4;
RA Zhang H., Javor G.T.;
RT "Regulation of the isofunctional genes ubiD and ubiX of the ubiquinone
RT biosynthetic pathway of Escherichia coli.";
RL FEMS Microbiol. Lett. 223:67-72(2003).
RN [6]
RP FUNCTION.
RX PubMed=16923914; DOI=10.1128/jb.00668-06;
RA Gulmezian M., Zhang H., Javor G.T., Clarke C.F.;
RT "Genetic evidence for an interaction of the UbiG O-methyltransferase with
RT UbiX in Escherichia coli coenzyme Q biosynthesis.";
RL J. Bacteriol. 188:6435-6439(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=17889824; DOI=10.1016/j.abb.2007.08.009;
RA Gulmezian M., Hyman K.R., Marbois B.N., Clarke C.F., Javor G.T.;
RT "The role of UbiX in Escherichia coli coenzyme Q biosynthesis.";
RL Arch. Biochem. Biophys. 467:144-153(2007).
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 (By similarity). Acts in concert with
CC UbiD to perform the decarboxylation of 4-hydroxy-3-octaprenyl-benzoate,
CC a step in the biosynthesis of coenzyme Q (PubMed:16923914,
CC PubMed:17889824). {ECO:0000255|HAMAP-Rule:MF_01984,
CC ECO:0000269|PubMed:16923914, ECO:0000269|PubMed:17889824}.
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 -!- INDUCTION: During aerobic growth, expression depends on the carbon
CC source, with the highest expression on succinate, a median expression
CC on glycerol, and the lowest on glucose. During anaerobic growth,
CC glucose does not inhibit expression. {ECO:0000269|PubMed:12799002}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce very low levels
CC of coenzyme Q(8) during logarithmic growth, grow slowly on succinate as
CC the sole carbon source, accumulate 4-hydroxy-3-octaprenyl-benzoate, and
CC have reduced UbiG O-methyltransferase activity. In contrast, they
CC synthesize near normal levels of Q(8) in the stationary phase.
CC {ECO:0000269|PubMed:17889824}.
CC -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000255|HAMAP-
CC Rule:MF_01984}.
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DR EMBL; M68935; AAA23970.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75371.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16157.1; -; Genomic_DNA.
DR PIR; E65003; XMECFD.
DR RefSeq; NP_416814.1; NC_000913.3.
DR RefSeq; WP_000825700.1; NZ_STEB01000008.1.
DR AlphaFoldDB; P0AG03; -.
DR SMR; P0AG03; -.
DR BioGRID; 4260526; 357.
DR DIP; DIP-47873N; -.
DR IntAct; P0AG03; 6.
DR STRING; 511145.b2311; -.
DR PaxDb; P0AG03; -.
DR PRIDE; P0AG03; -.
DR EnsemblBacteria; AAC75371; AAC75371; b2311.
DR EnsemblBacteria; BAA16157; BAA16157; BAA16157.
DR GeneID; 60903993; -.
DR GeneID; 949033; -.
DR KEGG; ecj:JW2308; -.
DR KEGG; eco:b2311; -.
DR PATRIC; fig|511145.12.peg.2406; -.
DR EchoBASE; EB1037; -.
DR eggNOG; COG0163; Bacteria.
DR HOGENOM; CLU_074522_0_1_6; -.
DR InParanoid; P0AG03; -.
DR OMA; GATHIQD; -.
DR PhylomeDB; P0AG03; -.
DR BioCyc; EcoCyc:UBIX-MON; -.
DR BioCyc; MetaCyc:UBIX-MON; -.
DR PRO; PR:P0AG03; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0106141; F:flavin prenyltransferase activity; IDA:EcoCyc.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:EcoCyc.
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 2: Evidence at transcript level;
KW Flavoprotein; FMN; Prenyltransferase; Reference proteome; Transferase.
FT CHAIN 1..189
FT /note="Flavin prenyltransferase UbiX"
FT /id="PRO_0000134950"
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"
FT CONFLICT 62
FT /note="T -> S (in Ref. 1; AAA23970)"
FT /evidence="ECO:0000305"
FT CONFLICT 139..148
FT /note="AEIGAVIMPP -> GRNRCGDYAS (in Ref. 1; AAA23970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 20695 MW; 057255DB020BF5B4 CRC64;
MKRLIVGISG ASGAIYGVRL LQVLRDVTDI ETHLVMSQAA RQTLSLETDF SLREVQALAD
VTHDARDIAA SISSGSFQTL GMVILPCSIK TLSGIVHSYT DGLLTRAADV VLKERRPLVL
CVRETPLHLG HLRLMTQAAE IGAVIMPPVP AFYHRPQSLD DVINQTVNRV LDQFAITLPE
DLFARWQGA
