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PEC Original Annotations
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Essentiality
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Class
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non-essential
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References (PMID)
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Appl Environ Microbiol. 1995;61(7):2487-92.
Role of fadR and atoC(Con) mutations in poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthesis in recombinant pha+ Escherichia coli.
Rhie HG, Dennis D.
(
7618860
)
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Deletion
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OCR05
(D)
,
OCR05-12-1
(D)
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Related gene (W3110 PEC)
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Gene Search
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Search MG1655 PEC by gene name:
fadB
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Related strains
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Strains Search
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Search strains by gene name:
fadB
Search strains by all related name:
fadB b3846 ECK3838 f729 JW3822 oldB
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General information (Go to Linear View: )
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Gene Name
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fadB
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Alternative name
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b3846,ECK3838,f729,JW3822,oldB
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Location, Length
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4,026,805 - 4,028,994
(
-
)
;
86.79
min
;
2190
(bp) ,
729
(aa)
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Product
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fused 3-hydroxybutyryl-CoAepimerase/delta(3)-cis-delta(2)-trans-enoyl-CoAisomerase/enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase
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Operon Name
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fadBA
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Note
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4-enzyme protein: 3-hydroxyacyl-CoA dehydrogenase; 3-hydroxybutyryl-CoA epimerase; delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase; enoyl-CoA hydratase; GO_process: GO:0019395 - fatty acid oxidation
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Function
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enzyme; Degradation of small molecules: Fatty acids
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Gene Ontology
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GO:0003824
;
catalytic activity ( fadB )
GO:0003857
;
3-hydroxyacyl-CoA dehydrogenase activity ( fadB )
GO:0004165
;
dodecenoyl-CoA delta-isomerase activity ( fadB )
GO:0004300
;
enoyl-CoA hydratase activity ( fadB )
GO:0005488
;
binding ( fadB )
GO:0006629
;
lipid metabolic process ( fadB )
GO:0006631
;
fatty acid metabolic process ( fadB )
GO:0008152
;
metabolic process ( fadB )
GO:0008692
;
3-hydroxybutyryl-CoA epimerase activity ( fadB )
GO:0009062
;
fatty acid catabolic process ( fadB )
GO:0016042
;
lipid catabolic process ( fadB )
GO:0016491
;
oxidoreductase activity ( fadB )
GO:0016507
;
fatty acid beta-oxidation multienzyme complex ( fadB )
GO:0016829
;
lyase activity ( fadB )
GO:0016853
;
isomerase activity ( fadB )
GO:0050662
;
coenzyme binding ( fadB )
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PID
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1790281
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EC number
(KEGG Pathway)
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1.1.1.35
4.2.1.17
5.1.2.3
5.3.3.8
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Verified Protein Starts
(data
compiled from literature and appropriate citations are available from EcoGene)
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EcoGene
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fadB
(
EG10279
)
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Number of removed
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0 aa cleaved
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SWISS-PROT
(
Show simple
)
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Entry name(Acc.no)
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FADB_ECOLI
(
P21177
)
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- Protein name
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Fatty oxidation complex alpha subunit
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- Synonyms
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- Gene name
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Name=fadB; Synonyms=oldB; OrderedLocusNames=b3846;
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- Comments
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FUNCTION:FadB and fadA are the alpha and beta subunits of the multifunctional enzyme complex of the fatty acid degradation cycle.
CATALYTIC ACTIVITY:(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH.
CATALYTIC ACTIVITY:(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O.
CATALYTIC ACTIVITY:(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
CATALYTIC ACTIVITY:3-cis-dodecenoyl-CoA = 2-trans-dodecenoyl-CoA.
PATHWAY:Fatty acid beta-oxidation cycle; second step.
SUBUNIT:Tetramer of two alpha chains and two beta chains.
SIMILARITY:In the N-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
SIMILARITY:In the C-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
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Entry name(Acc.no)
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Q8FBI2
(
Q8FBI2
)
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- Protein name
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Fatty oxidation complex alpha subunit.
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- Synonyms
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- Gene name
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Name=fadB; OrderedLocusNames=c4793;
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- Comments
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SIMILARITY:Belongs to the enoyl-CoA hydratase/isomerase family.
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Entry name(Acc.no)
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FADB_ECO57
(
Q8X8I2
)
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- Protein name
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Fatty oxidation complex alpha subunit
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- Synonyms
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- Gene name
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Name=fadB; Synonyms=oldB; OrderedLocusNames=z5367, ECs4774;
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- Comments
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FUNCTION:FadB and fadA are the alpha and beta subunits of the multifunctional enzyme complex of the fatty acid degradation cycle (By similarity).
CATALYTIC ACTIVITY:(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH.
CATALYTIC ACTIVITY:(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O.
CATALYTIC ACTIVITY:(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
CATALYTIC ACTIVITY:3-cis-dodecenoyl-CoA = 2-trans-dodecenoyl-CoA.
PATHWAY:Fatty acid beta-oxidation cycle; third step.
SUBUNIT:Tetramer of two alpha chains and two beta chains (By similarity).
SIMILARITY:In the N-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
SIMILARITY:In the C-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
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MMBR References
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J Bacteriol. 1990;172(11):6459-68.
Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes.
DiRusso CC.
(
1699931
)
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Nucleic Acids Res. 1990;18(21):6439
Nucleotide sequence between the fadB gene and the rrnA operon from Escherichia coli.
Nakahigashi K, Inokuchi H.
(
2243799
)
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Nucleic Acids Res. 1990;18(16):4937
Nucleotide sequence of the fadA and fadB genes from Escherichia coli.
Nakahigashi K, Inokuchi H.
(
2204034
)
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J Bacteriol. 1984;158(2):535-42.
Cloning, mapping, and expression of genes involved in the fatty acid-degradative multienzyme complex of Escherichia coli.
Spratt SK, Black PN, Ragozzino MM, Nunn WD.
(
6144665
)
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J Biol Chem. 1983;258:9780-9785
The large subunit of the fatty acid oxidation complex from Escherichia coli is a multifunctional polypeptide. Evidence for the existence of a fatty acid oxidation operon (fadAB) in Escherichia coli.
Yang, S.-Y., and H. Schulz.
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J Bacteriol. 1988;170(6):2543-8.
Evidence that the fadB gene of the fadAB operon of Escherichia coli encodes 3-hydroxyacyl-coenzyme A (CoA) epimerase, delta 3-cis-delta 2-trans-enoyl-CoA isomerase, and enoyl-CoA hydratase in addition to 3-hydroxyacyl-CoA dehydrogenase.
Yang SY, Li JM, He XY, Cosloy SD, Schulz H.
(
3286611
)
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J Biol Chem. 1990;265:10424-10429
Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon.
Yang, S.-Y., X.-Y. Yang, G. Healy-Louie, H. Schulz, and M. Elzinga.
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Science. 1992;257(5071):771-8.
Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes.
Daniels DL, Plunkett G 3rd, Burland VD, Blattner FR.
(
1379743
)
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| Sequences |
Amino acid
FASTA format
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0001 MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS DLKGLLLRSN KAAFIVGADI
0071 TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTIAAVN GYALGGGCEC VLATDYRLAT PDLRIGLPET
0141 KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGADQALK IGLVDGVVKA EKLVEGAKAV LRQAINGDLD
0211 WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV AQTAGKHYPA PITAVKTIEA AARFGREEAL NLENKSFVPL
0281 AHTNEARALV GIFLNDQYVK GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVV MKDINDKSLT
0351 LGMTEAAKLL NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDIVVEAV VENPKVKKAV LAETEQKVRQ
0421 DTVLASNTST IPISELANAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW ASKMGKTPIV
0491 VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL LDVVGIDTAH HAQAVMAAGF
0561 PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP KKEEDAAVED LLAEVSQPKR DFSEEEIIAR
0631 MMIPMVNEVV RCLEEGIIAT PAEADMALVY GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP
0701 EGLRNKARHN EPYYPPVEPA RPVGDLKTA
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Nucleotide
FASTA format
View sequence out neighbor 100bp
|
-100 cggcatttct ttaatctttt gtttgcatat
-070 ttttaacaca aaatacacac ttcgactcat ctggtacgac cagatcacct tgcggattca ggagactgac
0001 atgctttaca aaggcgacac cctgtacctt gactggctgg aagatggcat tgccgaactg gtatttgatg
0071 ccccaggttc agttaataaa ctcgacactg cgaccgtcgc cagcctcggc gaggccatcg gcgtgctgga
0141 acagcaatca gatctaaaag ggctgctgct gcgttcgaac aaagcagcct ttatcgtcgg tgctgatatc
0211 accgaatttt tgtccctgtt cctcgttcct gaagaacagt taagtcagtg gctgcacttt gccaatagcg
0281 tgtttaatcg cctggaagat ctgccggtgc cgaccattgc tgccgtcaat ggctatgcgc tgggcggtgg
0351 ctgcgaatgc gtgctggcga ccgattatcg tctggcgacg ccggatctgc gcatcggtct gccggaaacc
0421 aaactgggca tcatgcctgg ctttggcggt tctgtacgta tgccacgtat gctgggcgct gacagtgcgc
0491 tggaaatcat tgccgccggt aaagatgtcg gcgcggatca ggcgctgaaa atcggtctgg tggatggcgt
0561 agtcaaagca gaaaaactgg ttgaaggcgc aaaggcggtt ttacgccagg ccattaacgg cgacctcgac
0631 tggaaagcaa aacgtcagcc gaagctggaa ccactaaaac tgagcaagat tgaagccacc atgagcttca
0701 ccatcgctaa agggatggtc gcacaaacag cggggaaaca ttatccggcc cccatcaccg cagtaaaaac
0771 cattgaagct gcggcccgtt ttggtcgtga agaagcctta aacctggaaa acaaaagttt tgtcccgctg
0841 gcgcatacca acgaagcccg cgcactggtc ggcattttcc ttaacgatca atatgtaaaa ggcaaagcga
0911 agaaactcac caaagacgtt gaaaccccga aacaggccgc ggtgctgggt gcaggcatta tgggcggcgg
0981 catcgcttac cagtctgcgt ggaaaggcgt gccggttgtc atgaaagata tcaacgacaa gtcgttaacc
1051 ctcggcatga ccgaagccgc gaaactgctg aacaagcagc ttgagcgcgg caagatcgat ggtctgaaac
1121 tggctggcgt gatctccaca atccacccaa cgctcgacta cgccggattt gaccgcgtgg atattgtggt
1191 agaagcggtt gttgaaaacc cgaaagtgaa aaaagccgta ctggcagaaa ccgaacaaaa agtacgccag
1261 gataccgtgc tggcgtctaa cacttcaacc attcctatca gcgaactggc caacgcgctg gaacgcccgg
1331 aaaacttctg cgggatgcac ttctttaacc cggtccaccg aatgccgttg gtagaaatta ttcgcggcga
1401 gaaaagctcc gacgaaacca tcgcgaaagt tgtcgcctgg gcgagcaaga tgggcaagac gccgattgtg
1471 gttaacgact gccccggctt ctttgttaac cgcgtgctgt tcccgtattt cgccggtttc agccagctgc
1541 tgcgcgacgg cgcggatttc cgcaagatcg acaaagtgat ggaaaaacag tttggctggc cgatgggccc
1611 ggcatatctg ctggacgttg tgggcattga taccgcgcat cacgctcagg ctgtcatggc agcaggcttc
1681 ccgcagcgga tgcagaaaga ttaccgcgat gccatcgacg cgctgtttga tgccaaccgc tttggtcaga
1751 agaacggcct cggtttctgg cgttataaag aagacagcaa aggtaagccg aagaaagaag aagacgccgc
1821 cgttgaagac ctgctggcag aagtgagcca gccgaagcgc gatttcagcg aagaagagat tatcgcccgc
1891 atgatgatcc cgatggtcaa cgaagtggtg cgctgtctgg aggaaggcat tatcgccact ccggcggaag
1961 cggatatggc gctggtctac ggcctgggct tccctccgtt ccacggcggc gcgttccgct ggctggacac
2031 cctcggtagc gcaaaatacc tcgatatggc acagcaatat cagcacctcg gcccgctgta tgaagtgccg
2101 gaaggtctgc gtaataaagc gcgtcataac gaaccgtact atcctccggt tgagccagcc cgtccggttg
2171 gcgacctgaa aacggcttaa ggagtcacaa tggaacaggt tgtcattgtc gatgcaattc gcaccccgat
2241 gggccgttcg aagggcggtg cttttcgtaa cgtgcgtgca gaagatctct
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