Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P12998

- BIOF_ECOLI

UniProt

P12998 - BIOF_ECOLI

Protein

8-amino-7-oxononanoate synthase

Gene

bioF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate, but it is believed that pimeloyl-ACP rather than pimeloyl-CoA is the physiological substrate of BioF.1 Publication

    Catalytic activityi

    Pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein].1 Publication

    Cofactori

    Pyridoxal phosphate.1 Publication

    Enzyme regulationi

    Competitively inhibited by D-alanine, 8-amino-7-hydroxy-8-phosphonononanoic acid and 2-amino-3-hydroxy-2-methylnonadioic acid.1 Publication

    Kineticsi

    1. KM=25 µM for pimeloyl-CoA (at pH 7.5 and at 30 degrees Celsius)1 Publication
    2. KM=0.5 µM for L-alanine (at pH 7.5 and at 30 degrees Celsius)1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 211Substrate1 Publication
    Binding sitei133 – 1331Substrate1 Publication
    Binding sitei179 – 1791Pyridoxal phosphate1 Publication
    Binding sitei352 – 3521Substrate1 Publication

    GO - Molecular functioni

    1. 8-amino-7-oxononanoate synthase activity Source: EcoCyc
    2. pyridoxal phosphate binding Source: UniProtKB

    GO - Biological processi

    1. biotin biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Biotin biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:7KAPSYN-MONOMER.
    ECOL316407:JW0759-MONOMER.
    MetaCyc:7KAPSYN-MONOMER.
    UniPathwayiUPA00078.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    8-amino-7-oxononanoate synthase (EC:2.3.1.47)
    Short name:
    AONS
    Alternative name(s):
    7-keto-8-amino-pelargonic acid synthase
    Short name:
    7-KAP synthase
    Short name:
    KAPA synthase
    8-amino-7-ketopelargonate synthase
    Gene namesi
    Name:bioF
    Ordered Locus Names:b0776, JW0759
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10121. bioF.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 3843838-amino-7-oxononanoate synthasePRO_0000163811Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei236 – 2361N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiP12998.
    PRIDEiP12998.

    Expressioni

    Gene expression databases

    GenevestigatoriP12998.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    DIPiDIP-6870N.
    IntActiP12998. 2 interactions.
    STRINGi511145.b0776.

    Structurei

    Secondary structure

    1
    384
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1311
    Helixi16 – 183
    Beta strandi30 – 367
    Beta strandi39 – 435
    Helixi52 – 543
    Helixi56 – 6914
    Turni77 – 804
    Helixi84 – 9714
    Beta strandi100 – 1067
    Helixi108 – 11912
    Beta strandi125 – 1295
    Helixi134 – 1418
    Beta strandi143 – 1508
    Helixi155 – 1639
    Beta strandi170 – 1778
    Turni179 – 1813
    Helixi187 – 19610
    Beta strandi200 – 2045
    Turni206 – 2116
    Helixi214 – 2163
    Helixi219 – 2224
    Beta strandi228 – 2369
    Beta strandi243 – 2475
    Helixi249 – 25810
    Helixi260 – 2634
    Beta strandi264 – 2663
    Helixi270 – 28415
    Helixi286 – 30621
    Beta strandi309 – 3113
    Beta strandi318 – 3203
    Beta strandi323 – 3275
    Helixi328 – 34013
    Turni350 – 3523
    Beta strandi358 – 3603
    Helixi370 – 38314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BS0X-ray1.65A1-384[»]
    1DJ9X-ray2.00A1-384[»]
    1DJEX-ray1.71A1-384[»]
    2G6WX-ray2.14A1-384[»]
    ProteinModelPortaliP12998.
    SMRiP12998. Positions 2-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12998.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni108 – 1092Pyridoxal phosphate binding
    Regioni204 – 2074Pyridoxal phosphate binding
    Regioni233 – 2364Pyridoxal phosphate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0156.
    HOGENOMiHOG000221021.
    KOiK00652.
    OMAiRICLHAF.
    OrthoDBiEOG6Q8HZD.
    PhylomeDBiP12998.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01693. BioF_aminotrans_2.
    InterProiIPR001917. Aminotrans_II_pyridoxalP_BS.
    IPR004839. Aminotransferase_I/II.
    IPR004723. AONS_Archaea/Proteobacteria.
    IPR022834. AONS_Proteobacteria.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR00858. bioF. 1 hit.
    PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P12998-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSWQEKINAA LDARRAADAL RRRYPVAQGA GRWLVADDRQ YLNFSSNDYL    50
    GLSHHPQIIR AWQQGAEQFG IGSGGSGHVS GYSVVHQALE EELAEWLGYS 100
    RALLFISGFA ANQAVIAAMM AKEDRIAADR LSHASLLEAA SLSPSQLRRF 150
    AHNDVTHLAR LLASPCPGQQ MVVTEGVFSM DGDSAPLAEI QQVTQQHNGW 200
    LMVDDAHGTG VIGEQGRGSC WLQKVKPELL VVTFGKGFGV SGAAVLCSST 250
    VADYLLQFAR HLIYSTSMPP AQAQALRASL AVIRSDEGDA RREKLAALIT 300
    RFRAGVQDLP FTLADSCSAI QPLIVGDNSR ALQLAEKLRQ QGCWVTAIRP 350
    PTVPAGTARL RLTLTAAHEM QDIDRLLEVL HGNG 384
    Length:384
    Mass (Da):41,594
    Last modified:January 1, 1990 - v1
    Checksum:iD1AF5C054A5B4B06
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1892AE → R in CAA00968. 1 PublicationCurated

    Mass spectrometryi

    Molecular mass is 41464.4±4.5 Da from positions 2 - 384. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04423 Genomic DNA. Translation: AAA23516.1.
    A11542 Unassigned DNA. Translation: CAA00968.1.
    U00096 Genomic DNA. Translation: AAC73863.1.
    AP009048 Genomic DNA. Translation: BAE76363.1.
    PIRiD32025. SYECKP.
    RefSeqiNP_415297.1. NC_000913.3.
    YP_489049.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73863; AAC73863; b0776.
    BAE76363; BAE76363; BAE76363.
    GeneIDi12930959.
    945384.
    KEGGiecj:Y75_p0749.
    eco:b0776.
    PATRICi32116753. VBIEscCol129921_0802.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04423 Genomic DNA. Translation: AAA23516.1 .
    A11542 Unassigned DNA. Translation: CAA00968.1 .
    U00096 Genomic DNA. Translation: AAC73863.1 .
    AP009048 Genomic DNA. Translation: BAE76363.1 .
    PIRi D32025. SYECKP.
    RefSeqi NP_415297.1. NC_000913.3.
    YP_489049.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BS0 X-ray 1.65 A 1-384 [» ]
    1DJ9 X-ray 2.00 A 1-384 [» ]
    1DJE X-ray 1.71 A 1-384 [» ]
    2G6W X-ray 2.14 A 1-384 [» ]
    ProteinModelPortali P12998.
    SMRi P12998. Positions 2-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6870N.
    IntActi P12998. 2 interactions.
    STRINGi 511145.b0776.

    Proteomic databases

    PaxDbi P12998.
    PRIDEi P12998.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73863 ; AAC73863 ; b0776 .
    BAE76363 ; BAE76363 ; BAE76363 .
    GeneIDi 12930959.
    945384.
    KEGGi ecj:Y75_p0749.
    eco:b0776.
    PATRICi 32116753. VBIEscCol129921_0802.

    Organism-specific databases

    EchoBASEi EB0119.
    EcoGenei EG10121. bioF.

    Phylogenomic databases

    eggNOGi COG0156.
    HOGENOMi HOG000221021.
    KOi K00652.
    OMAi RICLHAF.
    OrthoDBi EOG6Q8HZD.
    PhylomeDBi P12998.

    Enzyme and pathway databases

    UniPathwayi UPA00078 .
    BioCyci EcoCyc:7KAPSYN-MONOMER.
    ECOL316407:JW0759-MONOMER.
    MetaCyc:7KAPSYN-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P12998.
    PROi P12998.

    Gene expression databases

    Genevestigatori P12998.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPi MF_01693. BioF_aminotrans_2.
    InterProi IPR001917. Aminotrans_II_pyridoxalP_BS.
    IPR004839. Aminotransferase_I/II.
    IPR004723. AONS_Archaea/Proteobacteria.
    IPR022834. AONS_Proteobacteria.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    Pfami PF00155. Aminotran_1_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR00858. bioF. 1 hit.
    PROSITEi PS00599. AA_TRANSFER_CLASS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon."
      Otsuka A.J., Buoncristiani M.R., Howard P.K., Flamm J., Johnson O., Yamamoto R., Uchida K., Cook C., Ruppert J., Matsuzaki J.
      J. Biol. Chem. 263:19577-19585(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Genetic material for expression of biotin synthetase enzymes."
      Pearson B.M., McKee R.A.
      Patent number GB2216530, 11-OCT-1989
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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.
    5. "Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies."
      Webster S.P., Alexeev D., Campopiano D.J., Watt R.M., Alexeeva M., Sawyer L., Baxter R.L.
      Biochemistry 39:516-528(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-6, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MASS SPECTROMETRY, REACTION MECHANISM.
    6. "Slow-binding and competitive inhibition of 8-amino-7-oxopelargonate synthase, a pyridoxal-5'-phosphate-dependent enzyme involved in biotin biosynthesis, by substrate and intermediate analogs. Kinetic and binding studies."
      Ploux O., Breyne O., Carillon S., Marquet A.
      Eur. J. Biochem. 259:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. "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, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
    8. "The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme."
      Alexeev D., Alexeeva M., Baxter R.L., Campopiano D.J., Webster S.P., Sawyer L.
      J. Mol. Biol. 284:401-419(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), SUBUNIT.
    9. "Suicide inhibition of alpha-oxamine synthases: structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanine."
      Alexeev D., Baxter R.L., Campopiano D.J., Kerbarh O., Sawyer L., Tomczyk N., Watt R., Webster S.P.
      Org. Biomol. Chem. 4:1209-1212(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.

    Entry informationi

    Entry nameiBIOF_ECOLI
    AccessioniPrimary (citable) accession number: P12998
    Secondary accession number(s): Q2MBJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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