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Escherichia coli K-12 substr. MG1655 Polypeptide: putative oxidoreductase, Fe-S subunit



Gene: aegA Accession Numbers: EG12409 (EcoCyc), b2468, ECK2463

Synonyms: yffG

Regulation Summary Diagram: ?

Summary:
AegA has C-terminal similarity to GltD and N-terminal similarity to iron-sulfur proteins [Cavicchioli96].

An aegA mutant does not have obvious phenotypes with respect to respiration or fermentation [Cavicchioli96]. The mutant also shows no defect in metabolizing ammonium or various amino acids (L-alanine, L-arginine, L-glutamic acid, glycine, or DL-serine) as a source of nitrogen, or in use of various sources of carbon [Cavicchioli96].

AegA, "anaerobically expressed gene" [Cavicchioli96].

Regulation has been described [Cavicchioli96]. The aegA gene is regulated by Fnr, NarXL, and NarQ (but not ArcA), induced under anaerobic conditions and repressed in the presence of nitrate (anaerobic) [Cavicchioli96].

Locations: cytosol

Map Position: [2,581,568 <- 2,583,547] (55.64 centisomes)
Length: 1980 bp / 659 aa

Molecular Weight of Polypeptide: 71.844 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0008127 , DIP:DIP-9060N , EchoBASE:EB2308 , EcoGene:EG12409 , EcoliWiki:b2468 , ModBase:P37127 , OU-Microarray:b2468 , PortEco:aegA , PR:PRO_000022062 , Pride:P37127 , Protein Model Portal:P37127 , RefSeq:NP_416963 , RegulonDB:EG12409 , SMR:P37127 , String:511145.b2468 , UniProt:P37127

Relationship Links: InterPro:IN-FAMILY:IPR001450 , InterPro:IN-FAMILY:IPR006006 , InterPro:IN-FAMILY:IPR012285 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR017896 , InterPro:IN-FAMILY:IPR017900 , InterPro:IN-FAMILY:IPR023753 , InterPro:IN-FAMILY:IPR028261 , Pfam:IN-FAMILY:PF00037 , Pfam:IN-FAMILY:PF07992 , Pfam:IN-FAMILY:PF14691 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS51379

In Paralogous Gene Group: 223 (21 members) , 381 (3 members)

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006537 - glutamate biosynthetic process Inferred by computational analysis [GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016639 - oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Inferred by computational analysis [GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism

Essentiality data for aegA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Sequence Features

Feature Class Location Citations Comment
Conserved-Region 3 -> 32
[UniProt09]
UniProt: 4Fe-4S ferredoxin-type 1;
Metal-Binding-Site 12
[UniProt10a]
UniProt: Iron-sulfur 1 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 15
[UniProt10a]
UniProt: Iron-sulfur 1 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 18
[UniProt10a]
UniProt: Iron-sulfur 1 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 22
[UniProt10a]
UniProt: Iron-sulfur 2 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Conserved-Region 47 -> 77
[UniProt09]
UniProt: 4Fe-4S ferredoxin-type 2;
Metal-Binding-Site 56
[UniProt10a]
UniProt: Iron-sulfur 3 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 59
[UniProt10a]
UniProt: Iron-sulfur 3 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 64
[UniProt10a]
UniProt: Iron-sulfur 3 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 68
[UniProt10a]
UniProt: Iron-sulfur 4 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Conserved-Region 78 -> 107
[UniProt09]
UniProt: 4Fe-4S ferredoxin-type 3;
Metal-Binding-Site 87
[UniProt10a]
UniProt: Iron-sulfur 4 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 90
[UniProt10a]
UniProt: Iron-sulfur 4 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 93
[UniProt10a]
UniProt: Iron-sulfur 4 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 97
[UniProt10a]
UniProt: Iron-sulfur 3 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Conserved-Region 114 -> 147
[UniProt09]
UniProt: 4Fe-4S ferredoxin-type 4;
Metal-Binding-Site 121
[UniProt10a]
UniProt: Iron-sulfur 2 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 124
[UniProt10a]
UniProt: Iron-sulfur 2 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 133
[UniProt10a]
UniProt: Iron-sulfur 2 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 137
[UniProt10a]
UniProt: Iron-sulfur 1 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Sequence-Conflict 488
[Cavicchioli96, UniProt10]
Alternate sequence: L → R; UniProt: (in Ref. 1; AAB46944);
Sequence-Conflict 513
[Cavicchioli96, UniProt10]
Alternate sequence: V → A; UniProt: (in Ref. 1; AAB46944);
Sequence-Conflict 600
[Cavicchioli96, UniProt10]
Alternate sequence: W → M; UniProt: (in Ref. 1);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b2468 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12409; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Cavicchioli96: Cavicchioli R, Kolesnikow T, Chiang RC, Gunsalus RP (1996). "Characterization of the aegA locus of Escherichia coli: control of gene expression in response to anaerobiosis and nitrate." J Bacteriol 178(23);6968-74. PMID: 8955321

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

Raghavan11a: Raghavan R, Sage A, Ochman H (2011). "Genome-wide identification of transcription start sites yields a novel thermosensing RNA and new cyclic AMP receptor protein-regulated genes in Escherichia coli." J Bacteriol 193(11);2871-4. PMID: 21460078


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Nov 24, 2014, BIOCYC14B.