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UniProtKB/Swiss-Prot entry P0AEK4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FABI_ECOLI
Primary accession number P0AEK4
Secondary accession number P29132
Integrated into Swiss-Prot on December 20, 2005
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 38)
Name and origin of the protein
Protein name Enoyl-[acyl-carrier-protein] reductase [NADH]
Synonyms EC 1.3.1.9
NADH-dependent enoyl-ACP reductase
Gene name
Name: fabI
Synonyms: envM
OrderedLocusNames: b1288, JW1281
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31, AND MUTAGENESIS.
PubMed=1364817 [NCBI, ExPASy, EBI, Israel, Japan]
Bergler H., Hoegenauer G., Turnowsky F.;
"Sequences of the envM gene and of two mutated alleles in Escherichia coli.";
J. Gen. Microbiol. 138:2093-2100(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1007/BF00028873; PubMed=8075395 [NCBI, ExPASy, EBI, Israel, Japan]
Kater M.M., Koningstein G.M., Nijkamp H.J.J., Stuitje A.R.;
"The use of a hybrid genetic system to study the functional relationship between prokaryotic and plant multi-enzyme fatty acid synthetase complexes.";
Plant Mol. Biol. 25:771-790(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan]
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
PubMed=8119879 [NCBI, ExPASy, EBI, Israel, Japan]
Bergler H., Wallner P., Ebeling A., Leitinger B., Fuchsbichler S., Aschauer H., Kollenz G., Hoegenauer G., Turnowsky F.;
"Protein EnvM is the NADH-dependent enoyl-ACP reductase (FabI) of Escherichia coli.";
J. Biol. Chem. 269:5493-5496(1994).
[7]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[8]
PROTEIN SEQUENCE OF 2-12.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
Submitted (FEB-1996) to UniProtKB.
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1126/science.274.5295.2107; PubMed=8953047 [NCBI, ExPASy, EBI, Israel, Japan]
Baldock C., Rafferty J.B., Sedelnikova S.E., Baker P.J., Stuitje A.R., Slabas A.R., Hawkes T.R., Rice D.W.;
"A mechanism of drug action revealed by structural studies of enoyl reductase.";
Science 274:2107-2110(1996).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1021/bi9907779; PubMed=10493822 [NCBI, ExPASy, EBI, Israel, Japan]
Ward W.H., Holdgate G.A., Rowsell S., McLean E.G., Pauptit R.A., Clayton E., Nichols W.W., Colls J.G., Minshull C.A., Jude D.A., Mistry A., Timms D., Camble R., Hales N.J., Britton C.J., Taylor I.W.;
"Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan.";
Biochemistry 38:12514-12525(1999).
[11]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
DOI=10.1006/jmbi.1999.2907; PubMed=10398587 [NCBI, ExPASy, EBI, Israel, Japan]
Stewart M.J., Parikh S., Xiao G., Tonge P.J., Kisker C.;
"Structural basis and mechanism of enoyl reductase inhibition by triclosan.";
J. Mol. Biol. 290:859-865(1999).
[12]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1038/18803; PubMed=10201369 [NCBI, ExPASy, EBI, Israel, Japan]
Levy C.W., Roujeinikova A., Sedelnikova S., Baker P.J., Stuitje A.R., Slabas A.R., Rice D.W., Rafferty J.B.;
"Molecular basis of triclosan activity.";
Nature 398:383-384(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M97219; AAA17755.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X78733; CAA55381.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74370.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA14841.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S48029; S48029.
RefSeq AP_001914.1; -.
NP_415804.1; -.
3D structure databases
PDB
1C14; X-ray; 2.00 A; A/B=1-262.[ExPASy / RCSB / EBI]
1D8A; X-ray; 2.20 A; A/B=1-262.[ExPASy / RCSB / EBI]
1DFG; X-ray; 2.50 A; A/B=1-262.[ExPASy / RCSB / EBI]
1DFH; X-ray; 2.20 A; A/B=1-262.[ExPASy / RCSB / EBI]
1DFI; X-ray; 2.09 A; A/B/C/D=1-262.[ExPASy / RCSB / EBI]
1I2Z; X-ray; 2.80 A; A/B=1-262.[ExPASy / RCSB / EBI]
1I30; X-ray; 2.40 A; A/B=1-262.[ExPASy / RCSB / EBI]
1LX6; X-ray; 2.40 A; A/B=1-262.[ExPASy / RCSB / EBI]
1LXC; X-ray; 2.40 A; A/B=1-262.[ExPASy / RCSB / EBI]
1MFP; X-ray; 2.33 A; A/B=1-262.[ExPASy / RCSB / EBI]
1QG6; X-ray; 1.90 A; A/B/C/D=1-262.[ExPASy / RCSB / EBI]
1QSG; X-ray; 1.75 A; A/B/C/D/E/F/G/H=1-262.[ExPASy / RCSB / EBI]
2FHS; X-ray; 2.70 A; A/B=1-262.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1C14; -.
1D8A; -.
1DFG; -.
1DFH; -.
1DFI; -.
1I2Z; -.
1I30; -.
1LX6; -.
1LXC; -.
1MFP; -.
1QG6; -.
1QSG; -.
2FHS; -.
ModBase P0AEK4.
Protein-protein interaction databases
IntAct P0AEK4; 12.
Enzyme and pathway databases
BioCyc EcoCyc:ENOYL-ACP-REDUCT-NADH-MON; -.
MetaCyc:ENOYL-ACP-REDUCT-NADH-MON; -.
2D gel databases
SWISS-2DPAGE P0AEK4; -.
Organism-specific databases
EchoBASE EB1490; -.
EcoGene EG11528; fabI.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004318; Molecular function: enoyl-[acyl-carrier-protein] reductase (NADH) activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006633; Biological process: fatty acid biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0046677; Biological process: response to antibiotic (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR014358; Enoyl-ACP_rdct.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
PTHR19410:SF12; Enoyl-ACP_rdct; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
Genome annotation databases
GeneID 945870; -.
GenomeReviews AP009048_GR; JW1281.
U00096_GR; b1288.
KEGG ecj:JW1281; -.
eco:b1288; -.
Phylogenomic databases
HOGENOM P0AEK4; -.
Other
BindingDB P0AEK4; -.
LinkHub P0AEK4; -.
Genome annotation databases
CMR P0AEK4; b1288.
Other
ProtoNet P0AEK4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antibiotic resistance; Cell inner membrane; Cell membrane; Complete proteome; Direct protein sequencing; Fatty acid biosynthesis; Lipid synthesis; Membrane; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   262  261     Enoyl-[acyl-carrier-protein] reductase [NADH]. PRO_0000054899
NP_BIND   10    36  27     NAD (By similarity). 
BINDING   156   156        Substrate (By similarity). 
MUTAGEN   93    93        G->S: Diazaborine resistance. 
MUTAGEN   241   241        S->F: Produces temperature-sensitive phenotype. 
TURN   3     6  4      
STRAND   8    11  4      
HELIX   20    30  11      
STRAND   34    41  8      
TURN   42    44  3      
HELIX   45    54  10      
STRAND   60    62  3      
HELIX   68    79  12      
STRAND   83    90  8      
HELIX   97   100  4      
HELIX   104   107  4      
HELIX   110   120  11      
HELIX   122   131  10      
HELIX   132   134  3      
STRAND   135   145  11      
HELIX   147   149  3      
TURN   154   157  4      
HELIX   158   177  20      
HELIX   178   180  3      
STRAND   182   189  8      
HELIX   197   199  3      
HELIX   203   213  11      
HELIX   222   232  11      
HELIX   235   237  3      
STRAND   244   248  5      
HELIX   251   253  3      
Sequence information
Length: 262 AA [This is the length of the unprocessed precursor] Molecular weight: 27864 Da [This is the MW of the unprocessed precursor] CRC64: 436A89AF349D1866 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE FAAQLGSDIV 

        70         80         90        100        110        120 
LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL DGDYVNAVTR EGFKIAHDIS 

       130        140        150        160        170        180 
SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE RAIPNYNVMG LAKASLEANV RYMANAMGPE 

       190        200        210        220        230        240 
GVRVNAISAG PIRTLAASGI KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI 

       250        260 
SGEVVHVDGG FSIAAMNELE LK 

P0AEK4 in FASTA format

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