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discounted EARLY registration ends Dec 31, 2014
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12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
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MetaCyc Polypeptide: aldehyde dehydrogenase, FAD-binding subunit

Gene: yagS Accession Numbers: G6156 (MetaCyc), b0285, ECK0284

Synonyms: paoB

Species: Escherichia coli K-12 substr. MG1655

Component of: aldehyde dehydrogenase (extended summary available)

Summary:
YagS is predicted to be the FAD binding subunit of YagTSR aldehyde dehydrogenase [Neumann09].

Locations: periplasmic space

Map Position: [300,155 <- 301,111]

Molecular Weight of Polypeptide: 33.858 kD (from nucleotide sequence), 33.9 kD (experimental) [Neumann09 ]

Unification Links: ASAP:ABE-0000990 , EchoBASE:EB3328 , EcoGene:EG13558 , EcoliWiki:b0285 , ModBase:P77324 , OU-Microarray:b0285 , PortEco:yagS , Pride:P77324 , Protein Model Portal:P77324 , RefSeq:NP_414819 , RegulonDB:G6156 , SMR:P77324 , String:511145.b0285 , UniProt:P77324

Relationship Links: InterPro:IN-FAMILY:IPR002346 , InterPro:IN-FAMILY:IPR005107 , InterPro:IN-FAMILY:IPR016166 , InterPro:IN-FAMILY:IPR016167 , InterPro:IN-FAMILY:IPR016169 , Pfam:IN-FAMILY:PF00941 , Pfam:IN-FAMILY:PF03450 , Prosite:IN-FAMILY:PS51387 , Smart:IN-FAMILY:SM01092

Ortholog Links: EcoO157Cyc (Escherichia coli O157:H7 str. EDL933):YAGS

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006144 - purine nucleobase metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0006166 - purine ribonucleoside salvage Inferred by computational analysis [UniProtGOA11a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Neumann09]
GO:0016903 - oxidoreductase activity, acting on the aldehyde or oxo group of donors Inferred from experiment [Neumann09]
GO:0050660 - flavin adenine dinucleotide binding Inferred from experiment Inferred by computational analysis [GOA01a, Neumann09]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0004854 - xanthine dehydrogenase activity Inferred by computational analysis [GOA01]
GO:0008762 - UDP-N-acetylmuramate dehydrogenase activity Inferred by computational analysis [GOA01a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016614 - oxidoreductase activity, acting on CH-OH group of donors Inferred by computational analysis [GOA01a]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space
GO:0042597 - periplasmic space Author statement [Neumann09]

MultiFun Terms: cell processes protection detoxification

Credits:
Last-Curated ? 11-Jun-2009 by Mackie A , Macquarie University


Subunit of: aldehyde dehydrogenase

Synonyms: YagTSR, PaoABC

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of aldehyde dehydrogenase = [YagT][YagS][YagR]
         aldehyde dehydrogenase, Fe-S subunit = YagT (summary available)
         aldehyde dehydrogenase, FAD-binding subunit = YagS (summary available)
         aldehyde dehydrogenase: molybdenum cofactor-binding subunit = YagR (summary available)

Summary:
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]

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


Enzymatic reaction of: aldehyde dehydrogenase

EC Number: 1.2.99.7

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.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

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


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 1 -> 223
[UniProt09]
UniProt: FAD-binding PCMH-type;
Nucleotide-Phosphate-Binding-Region 26 -> 33
[UniProt10]
UniProt: FAD; Non-Experimental Qualifier: potential;
Nucleotide-Phosphate-Binding-Region 107 -> 111
[UniProt10]
UniProt: FAD; Non-Experimental Qualifier: potential;
Amino-Acid-Sites-That-Bind 212
[UniProt10]
UniProt: FAD; via amide nitrogen and carbonyl oxygen; Non-Experimental Qualifier: potential;
Amino-Acid-Sites-That-Bind 227
[UniProt10]
UniProt: FAD; Non-Experimental Qualifier: potential;

History:
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.


References

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

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

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.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 28, 2014, BIOCYC13A.