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Protein

Enoyl-[acyl-carrier-protein] reductase [NADH] FabI

Gene

fabI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis.3 Publications

Catalytic activityi

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.1 Publication

Enzyme regulationi

Inhibited by diazaborines, triclosan (5-chloro-2-2,4-dichlorophenoxyphenol), 1,4-disubstituted imidazoles, 1,4-benzodiazepine derivatives, naphthyridinone derivatives, luteolin and curcumin.9 Publications

Kineticsi

  1. KM=3.3 µM for trans-2-dodecenoyl-ACP (DD-ACP)(at 25 degrees Celsius and pH 8)2 Publications
  2. KM=22 µM for crotonyl-ACP (at 30 degrees Celsius and pH 7.5)2 Publications
  3. KM=24 µM for trans-2-dodecenoyl-CoA (DD-CoA)(at 25 degrees Celsius and pH 8)2 Publications
  4. KM=2700 µM for crotonyl-CoA (at 30 degrees Celsius and pH 7.5)2 Publications

    Pathway: fatty acid biosynthesis

    This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

    Pathway: biotin biosynthesis

    This protein is involved in the pathway biotin biosynthesis, which is part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway biotin biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei13 – 131NAD; via carbonyl oxygen8 Publications
    Binding sitei40 – 401NAD8 Publications
    Binding sitei92 – 921NAD; via carbonyl oxygen8 Publications
    Binding sitei95 – 951Substrate; via amide nitrogen and carbonyl oxygen
    Active sitei146 – 1461Proton acceptorBy similarity
    Active sitei156 – 1561Proton acceptorBy similarity
    Binding sitei163 – 1631NAD8 Publications
    Sitei201 – 2011Involved in acyl-ACP binding
    Sitei204 – 2041Involved in acyl-ACP binding
    Sitei205 – 2051Involved in acyl-ACP binding

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 202NAD8 Publications
    Nucleotide bindingi64 – 652NAD8 Publications
    Nucleotide bindingi192 – 1965NAD8 Publications

    GO - Molecular functioni

    • enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB
    • identical protein binding Source: EcoCyc

    GO - Biological processi

    • biotin biosynthetic process Source: UniProtKB
    • fatty acid elongation Source: UniProtKB
    • lipid biosynthetic process Source: EcoCyc
    • protein homotetramerization Source: UniProtKB
    • response to antibiotic Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Antibiotic resistance, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciEcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
    ECOL316407:JW1281-MONOMER.
    MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
    BRENDAi1.3.1.9. 2026.
    SABIO-RKP0AEK4.
    UniPathwayiUPA00078.
    UPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (EC:1.3.1.9)
    Short name:
    ENR
    Alternative name(s):
    NADH-dependent enoyl-ACP reductase
    Gene namesi
    Name:fabI
    Synonyms:envM
    Ordered Locus Names:b1288, JW1281
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11528. fabI.

    Subcellular locationi

    GO - Cellular componenti

    • membrane Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi93 – 931G → S: Diazaborine resistance. 2 Publications
    Mutagenesisi93 – 931G → V: Triclosan resistance. 2 Publications
    Mutagenesisi146 – 1461Y → F: Large impact on catalysis, with kcat and kcat/Km for DD-ACP decreasing by around 50-fold compared with wild-type. 1 Publication
    Mutagenesisi156 – 1561Y → F: No effect on substrate reduction. 1 Publication
    Mutagenesisi159 – 1591M → T: Triclosan resistance. 1 Publication
    Mutagenesisi201 – 2011K → A: No effect on substrate reduction. 1 Publication
    Mutagenesisi201 – 2011K → E: Little activity toward DD-CoA and DD-ACP. 1 Publication
    Mutagenesisi203 – 2031F → L: Triclosan resistance. 1 Publication
    Mutagenesisi204 – 2041R → A: No effect on substrate reduction. 1 Publication
    Mutagenesisi204 – 2041R → E: Causes a further reduction in kcat/Km for reduction of DD-ACP without affecting kcat/Km for the DD-CoA substrate. 1 Publication
    Mutagenesisi205 – 2051K → A: No effect on substrate reduction. 1 Publication
    Mutagenesisi205 – 2051K → E: Causes a further reduction in kcat/Km for reduction of DD-ACP without affecting kcat/Km for the DD-CoA substrate. Has a larger impact on substrate reduction. 1 Publication
    Mutagenesisi241 – 2411S → F: Produces temperature-sensitive phenotype.

    Chemistry

    DrugBankiDB08604. Triclosan.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 262261Enoyl-[acyl-carrier-protein] reductase [NADH] FabIPRO_0000054899Add
    BLAST

    Proteomic databases

    PaxDbiP0AEK4.
    PRIDEiP0AEK4.

    2D gel databases

    SWISS-2DPAGEP0AEK4.

    Interactioni

    Subunit structurei

    Homotetramer.8 Publications

    Protein-protein interaction databases

    DIPiDIP-31867N.
    IntActiP0AEK4. 12 interactions.
    MINTiMINT-1251203.
    STRINGi511145.b1288.

    Structurei

    Secondary structure

    1
    262
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni3 – 64Combined sources
    Beta strandi8 – 114Combined sources
    Beta strandi16 – 194Combined sources
    Helixi20 – 3011Combined sources
    Beta strandi34 – 418Combined sources
    Turni42 – 443Combined sources
    Helixi45 – 5410Combined sources
    Beta strandi60 – 623Combined sources
    Helixi68 – 7912Combined sources
    Beta strandi83 – 908Combined sources
    Helixi97 – 1004Combined sources
    Beta strandi101 – 1033Combined sources
    Helixi104 – 1074Combined sources
    Helixi110 – 12011Combined sources
    Helixi122 – 13110Combined sources
    Helixi132 – 1343Combined sources
    Beta strandi135 – 14511Combined sources
    Helixi147 – 1493Combined sources
    Turni154 – 1574Combined sources
    Helixi158 – 17720Combined sources
    Turni178 – 1814Combined sources
    Beta strandi182 – 1898Combined sources
    Helixi197 – 1993Combined sources
    Beta strandi200 – 2023Combined sources
    Helixi203 – 21311Combined sources
    Helixi222 – 23211Combined sources
    Helixi235 – 2373Combined sources
    Beta strandi244 – 2485Combined sources
    Helixi251 – 2533Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C14X-ray2.00A/B1-262[»]
    1D8AX-ray2.20A/B2-262[»]
    1DFGX-ray2.50A/B2-262[»]
    1DFHX-ray2.20A/B2-262[»]
    1DFIX-ray2.09A/B/C/D2-262[»]
    1I2ZX-ray2.80A/B1-262[»]
    1I30X-ray2.40A/B1-262[»]
    1LX6X-ray2.40A/B1-262[»]
    1LXCX-ray2.40A/B1-262[»]
    1MFPX-ray2.33A/B1-262[»]
    1QG6X-ray1.90A/B/C/D2-262[»]
    1QSGX-ray1.75A/B/C/D/E/F/G/H1-262[»]
    2FHSX-ray2.70A/B1-262[»]
    3PJDX-ray2.50A/B1-262[»]
    3PJEX-ray2.50A/B1-262[»]
    3PJFX-ray1.90A/B1-262[»]
    4JQCX-ray2.80A/B1-262[»]
    4JX8X-ray3.20A/B1-262[»]
    ProteinModelPortaliP0AEK4.
    SMRiP0AEK4. Positions 2-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AEK4.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0623.
    InParanoidiP0AEK4.
    KOiK00208.
    OMAiASACKRE.
    OrthoDBiEOG6HF644.
    PhylomeDBiP0AEK4.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
    PRINTSiPR00081. GDHRDH.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AEK4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE
    60 70 80 90 100
    FAAQLGSDIV LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL
    110 120 130 140 150
    DGDYVNAVTR EGFKIAHDIS SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE
    160 170 180 190 200
    RAIPNYNVMG LAKASLEANV RYMANAMGPE GVRVNAISAG PIRTLAASGI
    210 220 230 240 250
    KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI SGEVVHVDGG
    260
    FSIAAMNELE LK
    Length:262
    Mass (Da):27,864
    Last modified:January 23, 2007 - v2
    Checksum:i436A89AF349D1866
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M97219 Unassigned DNA. Translation: AAA17755.1.
    X78733 Genomic DNA. Translation: CAA55381.1.
    U00096 Genomic DNA. Translation: AAC74370.1.
    AP009048 Genomic DNA. Translation: BAA14841.1.
    PIRiS48029.
    RefSeqiNP_415804.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC74370; AAC74370; b1288.
    BAA14841; BAA14841; BAA14841.
    GeneIDi945870.
    KEGGiecj:Y75_p1263.
    eco:b1288.
    PATRICi32117844. VBIEscCol129921_1342.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M97219 Unassigned DNA. Translation: AAA17755.1.
    X78733 Genomic DNA. Translation: CAA55381.1.
    U00096 Genomic DNA. Translation: AAC74370.1.
    AP009048 Genomic DNA. Translation: BAA14841.1.
    PIRiS48029.
    RefSeqiNP_415804.1. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C14X-ray2.00A/B1-262[»]
    1D8AX-ray2.20A/B2-262[»]
    1DFGX-ray2.50A/B2-262[»]
    1DFHX-ray2.20A/B2-262[»]
    1DFIX-ray2.09A/B/C/D2-262[»]
    1I2ZX-ray2.80A/B1-262[»]
    1I30X-ray2.40A/B1-262[»]
    1LX6X-ray2.40A/B1-262[»]
    1LXCX-ray2.40A/B1-262[»]
    1MFPX-ray2.33A/B1-262[»]
    1QG6X-ray1.90A/B/C/D2-262[»]
    1QSGX-ray1.75A/B/C/D/E/F/G/H1-262[»]
    2FHSX-ray2.70A/B1-262[»]
    3PJDX-ray2.50A/B1-262[»]
    3PJEX-ray2.50A/B1-262[»]
    3PJFX-ray1.90A/B1-262[»]
    4JQCX-ray2.80A/B1-262[»]
    4JX8X-ray3.20A/B1-262[»]
    ProteinModelPortaliP0AEK4.
    SMRiP0AEK4. Positions 2-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-31867N.
    IntActiP0AEK4. 12 interactions.
    MINTiMINT-1251203.
    STRINGi511145.b1288.

    Chemistry

    BindingDBiP0AEK4.
    ChEMBLiCHEMBL2364678.
    DrugBankiDB08604. Triclosan.

    2D gel databases

    SWISS-2DPAGEP0AEK4.

    Proteomic databases

    PaxDbiP0AEK4.
    PRIDEiP0AEK4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74370; AAC74370; b1288.
    BAA14841; BAA14841; BAA14841.
    GeneIDi945870.
    KEGGiecj:Y75_p1263.
    eco:b1288.
    PATRICi32117844. VBIEscCol129921_1342.

    Organism-specific databases

    EchoBASEiEB1490.
    EcoGeneiEG11528. fabI.

    Phylogenomic databases

    eggNOGiCOG0623.
    InParanoidiP0AEK4.
    KOiK00208.
    OMAiASACKRE.
    OrthoDBiEOG6HF644.
    PhylomeDBiP0AEK4.

    Enzyme and pathway databases

    UniPathwayiUPA00078.
    UPA00094.
    BioCyciEcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
    ECOL316407:JW1281-MONOMER.
    MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
    BRENDAi1.3.1.9. 2026.
    SABIO-RKP0AEK4.

    Miscellaneous databases

    EvolutionaryTraceiP0AEK4.
    PROiP0AEK4.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
    PRINTSiPR00081. GDHRDH.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequences of the envM gene and of two mutated alleles in Escherichia coli."
      Bergler H., Hoegenauer G., Turnowsky F.
      J. Gen. Microbiol. 138:2093-2100(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31, MUTAGENESIS OF GLY-93.
    2. "The use of a hybrid genetic system to study the functional relationship between prokaryotic and plant multi-enzyme fatty acid synthetase complexes."
      Kater M.M., Koningstein G.M., Nijkamp H.J.J., Stuitje A.R.
      Plant Mol. Biol. 25:771-790(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Protein EnvM is the NADH-dependent enoyl-ACP reductase (FabI) of Escherichia coli."
      Bergler H., Wallner P., Ebeling A., Leitinger B., Fuchsbichler S., Aschauer H., Kollenz G., Hoegenauer G., Turnowsky F.
      J. Biol. Chem. 269:5493-5496(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN ENOYL-ACP REDUCTASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    8. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
      Submitted (FEB-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    9. "Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli."
      Heath R.J., Rock C.O.
      J. Biol. Chem. 270:26538-26542(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FATTY ACID BIOSYNTHESIS.
    10. Cited for: ENZYME REGULATION, MUTAGENESIS OF GLY-93; MET-159 AND PHE-203.
    11. "Novel enoyl-ACP reductase (FabI) potential inhibitors of Escherichia coli from Chinese medicine monomers."
      Yao J., Zhang Q., Min J., He J., Yu Z.
      Bioorg. Med. Chem. Lett. 20:56-59(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    12. "Biotin synthesis begins by hijacking the fatty acid synthetic pathway."
      Lin S., Hanson R.E., Cronan J.E.
      Nat. Chem. Biol. 6:682-688(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN BIOTIN BIOSYNTHESIS.
    13. "A mechanism of drug action revealed by structural studies of enoyl reductase."
      Baldock C., Rafferty J.B., Sedelnikova S.E., Baker P.J., Stuitje A.R., Slabas A.R., Hawkes T.R., Rice D.W.
      Science 274:2107-2110(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION, SUBUNIT.
    14. "Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan."
      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.
      Biochemistry 38:12514-12525(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION, SUBUNIT.
    15. "Structural basis and mechanism of enoyl reductase inhibition by triclosan."
      Stewart M.J., Parikh S., Xiao G., Tonge P.J., Kisker C.
      J. Mol. Biol. 290:859-865(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION, SUBUNIT.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR.
    17. "Molecular basis for triclosan activity involves a flipping loop in the active site."
      Qiu X., Janson C.A., Court R.I., Smyth M.G., Payne D.J., Abdel-Meguid S.S.
      Protein Sci. 8:2529-2532(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR.
    18. "1,4-Disubstituted imidazoles are potential antibacterial agents functioning as inhibitors of enoyl acyl carrier protein reductase (FabI)."
      Heerding D.A., Chan G., DeWolf W.E., Fosberry A.P., Janson C.A., Jaworski D.D., McManus E., Miller W.H., Moore T.D., Payne D.J., Qiu X., Rittenhouse S.F., Slater-Radosti C., Smith W., Takata D.T., Vaidya K.S., Yuan C.C., Huffman W.F.
      Bioorg. Med. Chem. Lett. 11:2061-2065(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION.
    20. Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION.
    21. "Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli."
      Rafi S., Novichenok P., Kolappan S., Zhang X., Stratton C.F., Rawat R., Kisker C., Simmerling C., Tonge P.J.
      J. Biol. Chem. 281:39285-39293(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), MUTAGENESIS OF TYR-146; TYR-156; LYS-201; ARG-204 AND LYS-205, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiFABI_ECOLI
    AccessioniPrimary (citable) accession number: P0AEK4
    Secondary accession number(s): P29132
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 96 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The antibiotic diazaborine interferes with the activity by binding to the protein and NAD.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.