RegulonDB RegulonDB 10.8: Gene Form
   

fabD gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

fabH fabD fabG TSS_1405 (cluster) TSS_1405 (cluster) TSS_1404 TSS_1404 TSS_1403 (cluster) TSS_1403 (cluster) TSS_1402 TSS_1402 TSS_1401 TSS_1401 TSS_1400 TSS_1400 TSS_1399 TSS_1399 TSS_1398 TSS_1398 TSS_1397 TSS_1397 TSS_1396 TSS_1396 TSS_1395 TSS_1395 TSS_1394 TSS_1394 TSS_1393 TSS_1393 TSS_1392 TSS_1392 TSS_1391 TSS_1391 TSS_1390 TSS_1390 TSS_1389 TSS_1389

Gene      
Name: fabD    Texpresso search in the literature
Synonym(s): ECK1078, EG11317, b1092, tfpA
Genome position(nucleotides): 1149728 --> 1150657 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
55.16
External database links:  
ASAP:
ABE-0003698
ECHOBASE:
EB1293
OU-MICROARRAY:
b1092
PortEco:
fabD
STRING:
511145.b1092
COLOMBOS: fabD


Product      
Name: [acyl-carrier-protein] S-malonyltransferase
Synonym(s): FabD, TfpA
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 32.417
Isoelectric point: 4.673
Motif(s):
 
Type Positions Sequence
2 -> 309 TQFAFVFPGQGSQTVGMLADMAASYPIVEETFAEASAALGYDLWALTQQGPAEELNKTWQTQPALLTASVALYRVWQQQGGKAPAMMAGHSLGEYSALVCAGVIDFADAVRLVEMRGKFMQEAVPEGTGAMAAIIGLDDASIAKACEEAAEGQVVSPVNFNSPGQVVIAGHKEAVERAGAACKAAGAKRALPLPVSVPSHCALMKPAADKLAVELAKITFNAPTVPVVNNVDVKCETNGDAIRDALVRQLYNPVQWTKSVEYMAAQGVEHLYEVGPGKVLTGLTKRIVDTLTASALNEPSAMAAALEL
6 -> 283 FVFPGQGSQTVGMLADMAASYPIVEETFAEASAALGYDLWALTQQGPAEELNKTWQTQPALLTASVALYRVWQQQGGKAPAMMAGHSLGEYSALVCAGVIDFADAVRLVEMRGKFMQEAVPEGTGAMAAIIGLDDASIAKACEEAAEGQVVSPVNFNSPGQVVIAGHKEAVERAGAACKAAGAKRALPLPVSVPSHCALMKPAADKLAVELAKITFNAPTVPVVNNVDVKCETNGDAIRDALVRQLYNPVQWTKSVEYMAAQGVEHLYEVGPGKVLTG

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.4 - fatty acids and phosphatidic acid
Gene Ontology Terms (GO)  
cellular_component GO:0005829 - cytosol
molecular_function GO:0016740 - transferase activity
GO:0016746 - transferase activity, transferring acyl groups
GO:0004314 - [acyl-carrier-protein] S-malonyltransferase activity
GO:0016419 - S-malonyltransferase activity
biological_process GO:0006629 - lipid metabolic process
GO:0006631 - fatty acid metabolic process
GO:0006633 - fatty acid biosynthetic process
Note(s): Note(s): ...[more].
Reference(s): [1] Heath RJ., et al., 1995
[2] Jeon E., et al., 2011
[3] Liang JL., et al., 2016
[4] Marcella AM., et al., 2016
[5] Marcella AM., et al., 2015
[6] Park SY., et al., 2012
[7] Semple KS., et al., 1975
[8] Subrahmanyam S., et al., 1998
[9] Villa F., et al., 2012
[10] Walenga RW., et al., 1980
[11] Xu HH., et al., 2006
[12] Yang Y., et al., 2015
[13] Yu X., et al., 2011
[14] Zhang X., et al., 2012
External database links:  
DIP:
DIP-47923N
ECOCYC:
MALONYL-COA-ACP-TRANSACYL-MONOMER
ECOLIWIKI:
b1092
INTERPRO:
IPR020801
INTERPRO:
IPR024925
INTERPRO:
IPR016036
INTERPRO:
IPR016035
INTERPRO:
IPR014043
INTERPRO:
IPR004410
INTERPRO:
IPR001227
PDB:
2G2Z
PDB:
2G2Y
PDB:
2G2O
PDB:
2G1H
PDB:
1MLA
PFAM:
PF00698
PRIDE:
P0AAI9
PRODB:
PRO_000022561
REFSEQ:
NP_415610
SMART:
SM00827
SMR:
P0AAI9
UNIPROT:
P0AAI9


Operon      
Name: yceD-rpmF-plsX-fabHDG-acpP-fabF         
Operon arrangement:
Transcription unit        Promoter
yceD-rpmF
yceD-rpmF
rpmF-plsX-fabHDG
plsX-fabHDG
fabHDG
acpP
acpP-fabF
fabDG-acpP
fabF
fabG-acpP


Transcriptional Regulation      
Display Regulation             
Activated by: FadR


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_1389 1149153 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1390 1149156 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1391 1149172 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1392 1149706 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1393 1150045 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1394 1150372 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1395 1150404 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1396 1150416 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1397 1150443 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1398 1150491 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1399 1150589 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1400 1150957 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1401 1151080 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1402 1151229 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1403 (cluster) 1151352 forward For this promoter, there
Read more >
[RS-EPT-CBR] [15]
  promoter TSS_1404 1151355 forward nd [RS-EPT-CBR] [15]
  promoter TSS_1405 (cluster) 1151357 forward For this promoter, there
Read more >
[RS-EPT-CBR] [15]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Heath RJ., Rock CO., 1995, Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli., J Biol Chem 270(44):26538-42

 [2] Jeon E., Lee S., Won JI., Han SO., Kim J., Lee J., 2011, Development of Escherichia coli MG1655 strains to produce long chain fatty acids by engineering fatty acid synthesis (FAS) metabolism., Enzyme Microb Technol 49(1):44-51

 [3] Liang JL., Guo LQ., Lin JF., He ZQ., Cai FJ., Chen JF., 2016, A novel process for obtaining pinosylvin using combinatorial bioengineering in Escherichia coli., World J Microbiol Biotechnol 32(6):102

 [4] Marcella AM., Barb AW., 2016, A rapid fluorometric assay for the S-malonyltransacylase FabD and other sulfhydryl utilizing enzymes., J Biol Methods 3(4)

 [5] Marcella AM., Jing F., Barb AW., 2015, Preparation of holo- and malonyl-[acyl-carrier-protein] in a manner suitable for analog development., Protein Expr Purif 115:39-45

 [6] Park SY., Jeon E., Lee S., Lee J., Lee T., Won JI., 2012, An analysis of the concentration change of intermediate metabolites by gene manipulation in fatty acid biosynthesis., Enzyme Microb Technol 51(2):95-9

 [7] Semple KS., Silbert DF., 1975, Mapping of the fabD locus for fatty acid biosynthesis in Escherichia coli., J Bacteriol 121(3):1036-46

 [8] Subrahmanyam S., Cronan JE., 1998, Overproduction of a functional fatty acid biosynthetic enzyme blocks fatty acid synthesis in Escherichia coli., J Bacteriol 180(17):4596-602

 [9] Villa F., Remelli W., Forlani F., Vitali A., Cappitelli F., 2012, Altered expression level of Escherichia coli proteins in response to treatment with the antifouling agent zosteric acid sodium salt., Environ Microbiol 14(7):1753-61

 [10] Walenga RW., Osborn MJ., 1980, Biosynthesis of lipid A. Formation of acyl-deficient lipopolysaccharides in Salmonella typhimurium and Escherichia coli., J Biol Chem 255(9):4257-63

 [11] Xu HH., Real L., Bailey MW., 2006, An array of Escherichia coli clones over-expressing essential proteins: a new strategy of identifying cellular targets of potent antibacterial compounds., Biochem Biophys Res Commun 349(4):1250-7

 [12] Yang Y., Lin Y., Li L., Linhardt RJ., Yan Y., 2015, Regulating malonyl-CoA metabolism via synthetic antisense RNAs for enhanced biosynthesis of natural products., Metab Eng 29:217-26

 [13] Yu X., Liu T., Zhu F., Khosla C., 2011, In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli., Proc Natl Acad Sci U S A 108(46):18643-8

 [14] Zhang X., Agrawal A., San KY., 2012, Improving fatty acid production in Escherichia coli through the overexpression of malonyl coA-acyl carrier protein transacylase., Biotechnol Prog 28(1):60-5

 [15] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


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