Escherichia coli K-12 substr. MG1655 Polypeptide: aldehyde dehydrogenase, Fe-S subunit

Gene: paoA Accession Numbers: G6157 (EcoCyc), b0286, ECK0285

Synonyms: yagT

Regulation Summary Diagram: ?

Regulation summary diagram for paoA

Component of: aldehyde dehydrogenase (extended summary available)

YagT is the iron binding subunit of YagTSR aldehyde dehydrogenase [Xi00, Neumann09]. A yagT single deletion mutant is unable to grow in the presence of cinnamaldehyde at pH 4.0 [Neumann09]. Yag T contains a twin arginine signal peptide for translocation to the periplasm [TullmanErcek07].

Locations: periplasmic space

Map Position: [301,108 <- 301,797] (6.49 centisomes, 23°)
Length: 690 bp / 229 aa

Molecular Weight of Polypeptide: 24.343 kD (from nucleotide sequence), 21.0 kD (experimental) [Neumann09 ]

Unification Links: ASAP:ABE-0000992 , EchoBASE:EB3329 , EcoGene:EG13559 , EcoliWiki:b0286 , ModBase:P77165 , OU-Microarray:b0286 , PortEco:yagT , Pride:P77165 , Protein Model Portal:P77165 , RefSeq:NP_414820 , RegulonDB:G6157 , SMR:P77165 , String:511145.b0286 , Swiss-Model:P77165 , UniProt:P77165

Relationship Links: InterPro:IN-FAMILY:IPR001041 , InterPro:IN-FAMILY:IPR002888 , InterPro:IN-FAMILY:IPR006058 , InterPro:IN-FAMILY:IPR006311 , InterPro:IN-FAMILY:IPR012675 , Pfam:IN-FAMILY:PF00111 , Pfam:IN-FAMILY:PF01799 , Prosite:IN-FAMILY:PS00197 , Prosite:IN-FAMILY:PS51085 , Prosite:IN-FAMILY:PS51318

In Paralogous Gene Group: 86 (5 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006144 - purine nucleobase metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0006166 - purine ribonucleoside salvage Inferred by computational analysis [UniProtGOA11]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06, Neumann09]
GO:0016903 - oxidoreductase activity, acting on the aldehyde or oxo group of donors Inferred from experiment [Neumann09]
GO:0051537 - 2 iron, 2 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Neumann09]
GO:0009055 - electron carrier activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11, GOA01]
Cellular Component: GO:0042597 - periplasmic space Inferred from experiment [TullmanErcek07]
GO:0030288 - outer membrane-bounded periplasmic space [TullmanErcek07]

MultiFun Terms: cell processes protection detoxification

Essentiality data for paoA 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]

Last-Curated ? 10-Jun-2009 by Mackie A , Macquarie University

Subunit of: aldehyde dehydrogenase

Synonyms: YagTSR, PaoABC

Subunit composition of aldehyde dehydrogenase = [PaoA][PaoB][PaoC]
         aldehyde dehydrogenase, Fe-S subunit = PaoA (summary available)
         aldehyde dehydrogenase, FAD-binding subunit = PaoB (summary available)
         aldehyde dehydrogenase: molybdenum cofactor-binding subunit = PaoC (summary available)

YagTSR is a periplasmic aldehyde oxidoreductase with a possible role in the detoxification of aldehydes. Purified YagTSR oxidises a broad spectrum of aldehydes with a preference for aromatic aldehydes such as vanillin and cinnemaldehyde [Neumann09]. Purines are not oxidised by YagTSR [Neumann09]. YagTSR binds the molybdopterin cytosine dinucleotide (MCD) form of molybdenum cofactor and contains two (2Fe2S) clusters per protein trimer [Neumann09]. Purified YagTSR shows no activity with cytochrome c, NAD+ or oxygen as terminal electron acceptor however spinach ferredoxin was able to accept electrons from reduced YagTSR in vitro leading to the suggestion that ferredoxin may be the terminal electron acceptor in vivo [Neumann09].

YagTSR requires the presence of YagQ for activity. YagTSR expressed in the absence of YagQ is inactive and lacks molybdenum cofactor [Neumann09]. Based on its similarity to XbhC from Rhodobacter capsulatus [Neumann07] YagQ is predicted to be involved in molybdenum modification and insertion into YagTSR [Neumann09].

YagR is the molybdenum cofactor containing subunit; YagS is the FAD binding subunit and YagT is the iron binding subunit. Single deletion mutations in each of the yagT, yagS and yagR genes resulted in complete impairment of cell growth in the presence of cinnamaldehyde at pH 4.0 but not at pH values of 6-7 [Neumann09].

Locations: periplasmic space

Molecular Weight: 135.0 kD (experimental) [Neumann09]

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred from experiment [Neumann09]
Molecular Function: GO:0016903 - oxidoreductase activity, acting on the aldehyde or oxo group of donors Inferred from experiment [Neumann09]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space [Neumann09]
GO:0042597 - periplasmic space Author statement [Neumann09]

Created 11-Jun-2009 by Mackie A , Macquarie University

Enzymatic reaction of: aldehyde dehydrogenase

EC Number:

an aldehyde[periplasmic space] + FAD[periplasmic space] + H2O[periplasmic space] <=> a carboxylate[periplasmic space] + FADH2[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

Cofactors or Prosthetic Groups: a [2Fe-2S] iron-sulfur cluster [Neumann09], FAD [Neumann09], cytidylyl molybdenum cofactor [Neumann09]

Sequence Features

Protein sequence of aldehyde dehydrogenase, Fe-S subunit with features indicated

Feature Class Location Citations Comment
Signal-Sequence 1 -> 53
UniProt: Tat-type signal; Non-Experimental Qualifier: potential;
Chain 54 -> 229
UniProt: Putative xanthine dehydrogenase yagT iron-sulfur-binding subunit;
Conserved-Region 61 -> 137
UniProt: 2Fe-2S ferredoxin-type;
Metal-Binding-Site 99
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 104
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 107
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: by similarity;

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


Peter D. Karp on Thu Jan 16, 2003:
Predicted gene function revised as a result of E. coli genome reannotation by Serres et al. [Serres01 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

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

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

Neumann07: Neumann M, Stocklein W, Walburger A, Magalon A, Leimkuhler S (2007). "Identification of a Rhodobacter capsulatus L-cysteine desulfurase that sulfurates the molybdenum cofactor when bound to XdhC and before its insertion into xanthine dehydrogenase." Biochemistry 46(33);9586-95. PMID: 17649978

Neumann09: Neumann M, Mittelstadt G, Iobbi-Nivol C, Saggu M, Lendzian F, Hildebrandt P, Leimkuhler S (2009). "A periplasmic aldehyde oxidoreductase represents the first molybdopterin cytosine dinucleotide cofactor containing molybdo-flavoenzyme from Escherichia coli." FEBS J 276(10);2762-74. PMID: 19368556

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Serres01: Serres MH, Gopal S, Nahum LA, Liang P, Gaasterland T, Riley M (2001). "A functional update of the Escherichia coli K-12 genome." Genome Biol 2(9);RESEARCH0035. PMID: 11574054

TullmanErcek07: Tullman-Ercek D, DeLisa MP, Kawarasaki Y, Iranpour P, Ribnicky B, Palmer T, Georgiou G (2007). "Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." J Biol Chem 282(11);8309-16. PMID: 17218314

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

UniProt10: 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."

Xi00: Xi H, Schneider BL, Reitzer L (2000). "Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage." J Bacteriol 182(19);5332-41. PMID: 10986234

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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