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Escherichia coli K-12 substr. MG1655 Enzyme: Fad I component of anaerobic fatty acid oxidation complex



Gene: fadI Accession Numbers: G7213 (EcoCyc), b2342, ECK2336

Synonyms: yfcY

Regulation Summary Diagram: ?

Component of: anaerobic fatty acid oxidation complex (summary available)

Subunit composition of Fad I component of anaerobic fatty acid oxidation complex = [FadI]2
         FadI monomer = FadI

Summary:
During anaerobic beta-oxidation of fatty acids FadI, FadJ, and FadK serve functions parallel to those of FadA, FadB, and FadD in the aerobic pathway [Campbell03].

FadJ and FadI exhibit partial functional redundancy with FadA and FadB under aerobic conditions and the two complexes are proposed to increase efficiency of the process by favoring substrates of different chain length [Campbell03].

A strain producing FadJ and FadI from a plasmid exhibits thiolase activity with beta-ketyoacyl-CoAs of 6 to 12 carbon units but not with acetoacetyl-CoA [Snell02]. FadJ and FadI copurify over a gel filtration column [Snell02].

Regulation has been described [Campbell03]. FadR represses transcription of yfcYX in the presence of oxygen [Campbell03].

Locations: cytosol

Map Position: [2,457,181 <- 2,458,491] (52.96 centisomes)
Length: 1311 bp / 436 aa

Molecular Weight of Polypeptide: 46.531 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0007725 , DIP:DIP-11991N , EchoBASE:EB3880 , EcoGene:EG14128 , EcoliWiki:b2342 , ModBase:P76503 , OU-Microarray:b2342 , PortEco:fadI , Pride:P76503 , Protein Model Portal:P76503 , RefSeq:NP_416844 , RegulonDB:G7213 , SMR:P76503 , String:511145.b2342 , Swiss-Model:P76503 , UniProt:P76503

Relationship Links: InterPro:IN-FAMILY:IPR002155 , InterPro:IN-FAMILY:IPR012806 , InterPro:IN-FAMILY:IPR016038 , InterPro:IN-FAMILY:IPR016039 , InterPro:IN-FAMILY:IPR020610 , InterPro:IN-FAMILY:IPR020613 , InterPro:IN-FAMILY:IPR020615 , InterPro:IN-FAMILY:IPR020616 , InterPro:IN-FAMILY:IPR020617 , Panther:IN-FAMILY:PTHR18919 , Pfam:IN-FAMILY:PF00108 , Pfam:IN-FAMILY:PF02803 , Prosite:IN-FAMILY:PS00098 , Prosite:IN-FAMILY:PS00099 , Prosite:IN-FAMILY:PS00737

In Paralogous Gene Group: 286 (5 members)

Gene-Reaction Schematic: ?

Instance reaction of [a cis-3-enoyl-CoA ↔ a trans-2-enoyl-CoA] (5.3.3.8):
i2: 3-cis-dodecenoyl-CoA = 2-trans-dodecenoyl-CoA (5.3.3.8)

Instance reaction of [a (3S)-3-hydroxyacyl-CoA + NAD+ ↔ a 3-oxoacyl-CoA + NADH + H+] (1.1.1.35):
i1: 3-hydroxy-5-cis-tetradecenoyl-CoA + NAD+ = 3-keto-5-cis-tetradecenoyl-CoA + NADH + H+ (1.1.1.211)

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0033542 - fatty acid beta-oxidation, unsaturated, even number Inferred from experiment [Campbell03]
GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0006631 - fatty acid metabolic process Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0006635 - fatty acid beta-oxidation Inferred by computational analysis [UniProtGOA12]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0016042 - lipid catabolic process Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
Molecular Function: GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase activity Inferred from experiment [Snell02]
GO:0003988 - acetyl-CoA C-acyltransferase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Snell02]
GO:0004300 - enoyl-CoA hydratase activity Inferred from experiment [Snell02]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016746 - transferase activity, transferring acyl groups Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016747 - transferase activity, transferring acyl groups other than amino-acyl groups Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01a, Snell02]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]

MultiFun Terms: metabolism carbon utilization fatty acids

Essentiality data for fadI 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]
Yes [Feist07, Comment 4]

Enzymatic reaction of: acetyl-CoA C-acyltransferase (Fad I component of anaerobic fatty acid oxidation complex)

Synonyms: acyl-CoA:acetyl-CoA C-acyltransferase

EC Number: 2.3.1.16

a 2,3,4-saturated fatty acyl CoA + acetyl-CoA <=> a 3-oxoacyl-CoA + coenzyme A

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

The reaction is physiologically favored in the opposite direction.

In Pathways: fatty acid β-oxidation I


Subunit of: anaerobic fatty acid oxidation complex

Subunit composition of anaerobic fatty acid oxidation complex = [(FadJ)2][(FadI)2]
         FadJ component of anaerobic fatty acid oxidation complex = (FadJ)2
                 FadJ monomer = FadJ
         Fad I component of anaerobic fatty acid oxidation complex = (FadI)2
                 FadI monomer = FadI

Summary:
During anaerobic beta-oxidation of fatty acids FadI, FadJ, and FadK serve functions parallel to those of FadA, FadB, and FadD in the aerobic pathway [Campbell03].


Sequence Features

Feature Class Location Citations Comment
Active-Site 99
[UniProt10]
UniProt: Acyl-thioester intermediate; Non-Experimental Qualifier: by similarity;
Active-Site 392
[UniProt10]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;
Active-Site 422
[UniProt10]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


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

Campbell03: Campbell JW, Morgan-Kiss RM, E Cronan J (2003). "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway." Mol Microbiol 47(3);793-805. PMID: 12535077

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

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

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, 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."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

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

Snell02: Snell KD, Feng F, Zhong L, Martin D, Madison LL (2002). "YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from fatty acids in recombinant Escherichia coli fadB strains." J Bacteriol 184(20);5696-705. PMID: 12270828

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 the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

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

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Other References Related to Gene Regulation

Cho06: Cho BK, Knight EM, Palsson BO (2006). "Transcriptional regulation of the fad regulon genes of Escherichia coli by ArcA." Microbiology 152(Pt 8);2207-19. PMID: 16849788

Huerta03: Huerta AM, Collado-Vides J (2003). "Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals." J Mol Biol 333(2);261-78. PMID: 14529615


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, biocyc14.