GenePage for the apbE gene of Escherichia coli K-12

Primary Gene Name: apbE
EcoGene Accession Number: EG12073
K-12 Gene Accession Number: ECK2206
MG1655 Gene Identifier: b2214
Gene Name Mnemonic: Alternative pyrimidine biosynthesis
Alternate Gene Symbols: yojK; yojL
Description: Putative flavin transferase, lipoprotein
  # bp Upstream # bp Downstream
MW: 38548.82 ---------351 aa Pre-Run BlastP UniProt
Pre-Run BlastP NR+Env
Left End: 2310479
Left Intergenic Region

Name: ada_apbE

Length: 73 bp gap

Orientation: Codirectional-

Left_end: 2310406

Right_end: 2310478

Centisome: 49.78

Genomic Address
Counterclockwise
Minute or Centisome (%) = 49.78
Right End: 2311534
Right Intergenic Region

Name: apbE_ompC

Length: 111 bp gap

Orientation: Codirectional-

Left_end: 2311535

Right_end: 2311645

Centisome: 49.80

ApbE is probably required for a covalent flavination of conserved residues Thr187 in RsxD and Thr174 in RsxG with FMN, which then are likely to be required for the reduction of the 4Fe-4S cluster in ThiC in addition to the known Rsx function to reduce the 2Fe-2S cluster in SoxR. ApbE of Vibrio harveyi is a flavin transferase required for the covalent flavinylation of NqrC, an RsxG homolog, with FMN at position Thr229 (Bertsova, 2013). Vibrio cholerae RnfD (RsxD homolog) and RnfG (RsxG homolog) are covalently FMN flavinylated at residues Thr187 and Thr175, respectively (Backiel, 2008). Vibrio alginolyticus NqrC (RsxG homolog) and NqrB (RsxD homolog) are covalently FMN flavinylated at residues Thr223 and Thr235, respectively (Hayashi, 2001). ApbE of Salmonella typhimurium is required for the assembly or repair of 4Fe-4S clusters (Skovran, 2003). An apbE mutant of Salmonella typhimurium is blocked for thiamine biosynthesis at the ThiC step (conversion of AIR to HMP) and Salmonella ApbE is anchored to the inner membrane in a periplasmic location; the periplasmic location, but not the membrane anchor, is required for ApbE function (Beck, 1998; Beck, 1999). Purified E. coli ApbE is dimeric and, unlike the ApbE superfamily member TP0796 from Treponema pallidum, E. coli ApbE does not possess FAD pyrophosphatase activity in vitro (Deca, 2013). The structure of the S. enterica ApbE has a bound FAD molecule (Boyd, 2011). The first 19 aa of ApbE constitute a type II signal peptide.

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BamHI EcoRI HindIII