Difference between revisions of "Part:BBa K3038003"

(Reference)
(FadM_Cter-FLAG)
Line 1: Line 1:
  
===FadM_Cter-FLAG ===
+
==Description==
  
 +
FadM is for E. coli long-chain acyl CoA thioesterase that is Thioesterase III.<br/>
 +
Thioesterase III (FadM) is a long-chain acyl-CoA thioesterase that is involved in the β-oxidation of oleic acid. The enzyme is able to hydrolyze a number of related substrates. The best substrate is 3,5-tetradecadienoyl-CoA, which is a minor side product of oleate β-oxidation that is resistant to further degradation. The hydrolysis product, 3,5-tetradecadienoate, is released into the growth medium [Ren04a, Nie08]. Thioesterase III is expressed upon growth on oleic acid as the sole source of carbon [Ren04a, Nie08]. FadM is a member of the fad regulon; expression is induced by a number of fatty acids, with C18:1 as the best inducer [Feng09b]. Reports disagree on whether [Nie08a] or not [Feng09b] conjugated linoleic acid (CLA) induces an even higher level of expression of fadM.
  
FadM = E. coli long-chain acyl CoA thioesterase = Thioesterase III
+
https://biocyc.org/gene?orgid=ECOLI&id=G6244
 +
FadM_Cter-FLAG
 +
 
 +
===GenBank===
 +
 
 +
FadM : GenBank: P77712<br/>
 +
https://www.uniprot.org/uniprot/P77712
 +
 
 +
===Protein Sequence ===  
 +
 
 +
        10        20        30        40        50
 +
MQTQIKVRGY HLDVYQHVNN ARYLEFLEEA RWDGLENSDS FQWMTAHNIA
 +
        60        70        80        90        100
 +
FVVVNININY RRPAVLSDLL TITSQLQQLN GKSGILSQVI TLEPEGQVVA
 +
      110        120        130
 +
DALITFVCID LKTQKALALE GELREKLEQM VK
  
 
===Ecoli Long chain acyl CoA thioesterase ===
 
===Ecoli Long chain acyl CoA thioesterase ===

Revision as of 08:18, 19 October 2019

Description

FadM is for E. coli long-chain acyl CoA thioesterase that is Thioesterase III.
Thioesterase III (FadM) is a long-chain acyl-CoA thioesterase that is involved in the β-oxidation of oleic acid. The enzyme is able to hydrolyze a number of related substrates. The best substrate is 3,5-tetradecadienoyl-CoA, which is a minor side product of oleate β-oxidation that is resistant to further degradation. The hydrolysis product, 3,5-tetradecadienoate, is released into the growth medium [Ren04a, Nie08]. Thioesterase III is expressed upon growth on oleic acid as the sole source of carbon [Ren04a, Nie08]. FadM is a member of the fad regulon; expression is induced by a number of fatty acids, with C18:1 as the best inducer [Feng09b]. Reports disagree on whether [Nie08a] or not [Feng09b] conjugated linoleic acid (CLA) induces an even higher level of expression of fadM.

https://biocyc.org/gene?orgid=ECOLI&id=G6244 FadM_Cter-FLAG

GenBank

FadM : GenBank: P77712
https://www.uniprot.org/uniprot/P77712

Protein Sequence

       10         20         30         40         50

MQTQIKVRGY HLDVYQHVNN ARYLEFLEEA RWDGLENSDS FQWMTAHNIA

       60         70         80         90        100

FVVVNININY RRPAVLSDLL TITSQLQQLN GKSGILSQVI TLEPEGQVVA

      110        120        130 

DALITFVCID LKTQKALALE GELREKLEQM VK

Ecoli Long chain acyl CoA thioesterase

Thioesterase III

Thioesterase III (FadM) is a long-chain acyl-CoA thioesterase that is involved in the β-oxidation of oleic acid. The enzyme is able to hydrolyze a number of related substrates. The best substrate is 3,5-tetradecadienoyl-CoA, which is a minor side product of oleate β-oxidation that is resistant to further degradation. The hydrolysis product, 3,5-tetradecadienoate, is released into the growth medium [Ren04a, Nie08]. Thioesterase III is expressed upon growth on oleic acid as the sole source of carbon [Ren04a, Nie08]. fadM is a member of the fad regulon; expression is induced by a number of fatty acids, with C18:1 as the best inducer [Feng09b]. Reports disagree on whether [Nie08a] or not [Feng09b] conjugated linoleic acid (CLA) induces an even higher level of expression of fadM.

https://biocyc.org/gene?orgid=ECOLI&id=G6244


Protein Sequence

(not tagged) MQTQIKVRGY HLDVYQHVNN ARYLEFLEEA RWDGLENSDS FQWMTAHNIA FVVVNININY RRPAVLSDLL TITSQLQQLN GKSGILSQVI TLEPEGQVVA DALITFVCID LKTQKALALE GELREKLEQM VK


Molecular size : 15.088 kD (from nucleotide sequence)

Reference

Engineering of Bacterial Methyl Ketone Synthesis for Biofuels. Ee-Been Goh,a,c Edward E. K. Baidoo,a,c Jay D. Keasling,a,c,d and Harry R. Beller. Appl Environ Microbiol. 2012 Jan; 78(1): 70–80. doi: 10.1128/AEM.06785-11. PMCID: PMC3255637. PMID: 22038610

Usage and Biology

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]