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P0AEK4

- FABI_ECOLI

UniProt

P0AEK4 - FABI_ECOLI

Protein

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

Gene

fabI

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    Pathwayi

    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

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

    GO - Biological processi

    1. biotin biosynthetic process Source: UniProtKB
    2. fatty acid elongation Source: UniProtKB
    3. lipid biosynthetic process Source: EcoCyc
    4. protein homotetramerization Source: UniProtKB
    5. response to antibiotic Source: UniProtKB-KW

    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.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11528. fabI.

    Subcellular locationi

    GO - Cellular componenti

    1. membrane Source: UniProtKB

    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.

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AEK4.

    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 – 64
    Beta strandi8 – 114
    Beta strandi16 – 194
    Helixi20 – 3011
    Beta strandi34 – 418
    Turni42 – 443
    Helixi45 – 5410
    Beta strandi60 – 623
    Helixi68 – 7912
    Beta strandi83 – 908
    Helixi97 – 1004
    Beta strandi101 – 1033
    Helixi104 – 1074
    Helixi110 – 12011
    Helixi122 – 13110
    Helixi132 – 1343
    Beta strandi135 – 14511
    Helixi147 – 1493
    Turni154 – 1574
    Helixi158 – 17720
    Turni178 – 1814
    Beta strandi182 – 1898
    Helixi197 – 1993
    Beta strandi200 – 2023
    Helixi203 – 21311
    Helixi222 – 23211
    Helixi235 – 2373
    Beta strandi244 – 2485
    Helixi251 – 2533

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AEK4.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0623.
    KOiK00208.
    OMAiKLSIAWA.
    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

    MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE    50
    FAAQLGSDIV LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL 100
    DGDYVNAVTR EGFKIAHDIS SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE 150
    RAIPNYNVMG LAKASLEANV RYMANAMGPE GVRVNAISAG PIRTLAASGI 200
    KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI SGEVVHVDGG 250
    FSIAAMNELE LK 262
    Length:262
    Mass (Da):27,864
    Last modified:January 23, 2007 - v2
    Checksum:i436A89AF349D1866
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_489556.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74370; AAC74370; b1288.
    BAA14841; BAA14841; BAA14841.
    GeneIDi12931141.
    945870.
    KEGGiecj:Y75_p1263.
    eco:b1288.
    PATRICi32117844. VBIEscCol129921_1342.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S48029.
    RefSeqi NP_415804.1. NC_000913.3.
    YP_489556.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C14 X-ray 2.00 A/B 1-262 [» ]
    1D8A X-ray 2.20 A/B 2-262 [» ]
    1DFG X-ray 2.50 A/B 2-262 [» ]
    1DFH X-ray 2.20 A/B 2-262 [» ]
    1DFI X-ray 2.09 A/B/C/D 2-262 [» ]
    1I2Z X-ray 2.80 A/B 1-262 [» ]
    1I30 X-ray 2.40 A/B 1-262 [» ]
    1LX6 X-ray 2.40 A/B 1-262 [» ]
    1LXC X-ray 2.40 A/B 1-262 [» ]
    1MFP X-ray 2.33 A/B 1-262 [» ]
    1QG6 X-ray 1.90 A/B/C/D 2-262 [» ]
    1QSG X-ray 1.75 A/B/C/D/E/F/G/H 1-262 [» ]
    2FHS X-ray 2.70 A/B 1-262 [» ]
    3PJD X-ray 2.50 A/B 1-262 [» ]
    3PJE X-ray 2.50 A/B 1-262 [» ]
    3PJF X-ray 1.90 A/B 1-262 [» ]
    4JQC X-ray 2.80 A/B 1-262 [» ]
    4JX8 X-ray 3.20 A/B 1-262 [» ]
    ProteinModelPortali P0AEK4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-31867N.
    IntActi P0AEK4. 12 interactions.
    MINTi MINT-1251203.
    STRINGi 511145.b1288.

    Chemistry

    BindingDBi P0AEK4.
    ChEMBLi CHEMBL1857.

    2D gel databases

    SWISS-2DPAGE P0AEK4.

    Proteomic databases

    PaxDbi P0AEK4.
    PRIDEi P0AEK4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74370 ; AAC74370 ; b1288 .
    BAA14841 ; BAA14841 ; BAA14841 .
    GeneIDi 12931141.
    945870.
    KEGGi ecj:Y75_p1263.
    eco:b1288.
    PATRICi 32117844. VBIEscCol129921_1342.

    Organism-specific databases

    EchoBASEi EB1490.
    EcoGenei EG11528. fabI.

    Phylogenomic databases

    eggNOGi COG0623.
    KOi K00208.
    OMAi KLSIAWA.
    OrthoDBi EOG6HF644.
    PhylomeDBi P0AEK4.

    Enzyme and pathway databases

    UniPathwayi UPA00078 .
    UPA00094 .
    BioCyci EcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
    ECOL316407:JW1281-MONOMER.
    MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
    SABIO-RK P0AEK4.

    Miscellaneous databases

    EvolutionaryTracei P0AEK4.
    PROi P0AEK4.

    Gene expression databases

    Genevestigatori P0AEK4.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR014358. Enoyl-ACP_Rdtase_NADH.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PIRSFi PIRSF000094. Enoyl-ACP_rdct. 1 hit.
    PRINTSi PR00081. GDHRDH.
    ProtoNeti Search...

    Publicationsi

    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, COFACTOR.
    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: October 1, 2014
    This is version 89 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