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Protein

8-amino-7-oxononanoate synthase

Gene

bioF

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

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.2 Publications

Catalytic activityi

Pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein].2 Publications

Cofactori

pyridoxal 5'-phosphate1 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: biotin biosynthesis

    This protein is involved in the pathway biotin biosynthesis, which is part of Cofactor biosynthesis.1 Publication
    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)DescriptionActionsGraphical viewLength
    Binding sitei21Substrate1 Publication1
    Binding sitei133Substrate1 Publication1
    Binding sitei179Pyridoxal phosphate2 Publications1
    Binding sitei207Pyridoxal phosphate2 Publications1
    Binding sitei233Pyridoxal phosphate1 Publication1
    Binding sitei352Substrate1 Publication1

    GO - Molecular functioni

    • 8-amino-7-oxononanoate synthase activity Source: EcoCyc
    • pyridoxal phosphate binding Source: UniProtKB

    GO - Biological processi

    • biotin biosynthetic process Source: EcoCyc
    Complete GO annotation...

    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.
    BRENDAi2.3.1.47. 2026.
    SABIO-RKP12998.
    UniPathwayiUPA00078.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    8-amino-7-oxononanoate synthase1 Publication (EC:2.3.1.472 Publications)
    Short name:
    AONS1 Publication
    Alternative name(s):
    7-keto-8-amino-pelargonic acid synthase1 Publication
    Short name:
    7-KAP synthase1 Publication
    Short name:
    KAPA synthase1 Publication
    8-amino-7-ketopelargonate synthase
    Gene namesi
    Name:bioF1 Publication
    Ordered Locus Names:b0776, JW0759
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10121. bioF.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001638112 – 3848-amino-7-oxononanoate synthaseAdd BLAST383

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei236N6-(pyridoxal phosphate)lysine2 Publications1

    Proteomic databases

    PaxDbiP12998.
    PRIDEiP12998.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    BioGridi4259953. 17 interactors.
    DIPiDIP-6870N.
    IntActiP12998. 2 interactors.
    STRINGi511145.b0776.

    Structurei

    Secondary structure

    1384
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 13Combined sources11
    Helixi16 – 18Combined sources3
    Beta strandi30 – 36Combined sources7
    Beta strandi39 – 43Combined sources5
    Helixi52 – 54Combined sources3
    Helixi56 – 69Combined sources14
    Turni77 – 80Combined sources4
    Helixi84 – 97Combined sources14
    Beta strandi100 – 106Combined sources7
    Helixi108 – 119Combined sources12
    Beta strandi125 – 129Combined sources5
    Helixi134 – 141Combined sources8
    Beta strandi143 – 150Combined sources8
    Helixi155 – 163Combined sources9
    Beta strandi170 – 177Combined sources8
    Turni179 – 181Combined sources3
    Helixi187 – 196Combined sources10
    Beta strandi200 – 204Combined sources5
    Turni206 – 211Combined sources6
    Helixi214 – 216Combined sources3
    Helixi219 – 222Combined sources4
    Beta strandi228 – 236Combined sources9
    Beta strandi243 – 247Combined sources5
    Helixi249 – 258Combined sources10
    Helixi260 – 263Combined sources4
    Beta strandi264 – 266Combined sources3
    Helixi270 – 284Combined sources15
    Helixi286 – 306Combined sources21
    Beta strandi309 – 311Combined sources3
    Beta strandi318 – 320Combined sources3
    Beta strandi323 – 327Combined sources5
    Helixi328 – 340Combined sources13
    Turni350 – 352Combined sources3
    Beta strandi358 – 360Combined sources3
    Helixi370 – 383Combined sources14

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP12998.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni108 – 109Pyridoxal phosphate binding2 Publications2

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4107EEK. Bacteria.
    COG0156. LUCA.
    HOGENOMiHOG000221021.
    InParanoidiP12998.
    KOiK00652.
    OMAiELAHACI.
    PhylomeDBiP12998.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01693. BioF_aminotrans_2. 1 hit.
    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

            10         20         30         40         50
    MSWQEKINAA LDARRAADAL RRRYPVAQGA GRWLVADDRQ YLNFSSNDYL
    60 70 80 90 100
    GLSHHPQIIR AWQQGAEQFG IGSGGSGHVS GYSVVHQALE EELAEWLGYS
    110 120 130 140 150
    RALLFISGFA ANQAVIAAMM AKEDRIAADR LSHASLLEAA SLSPSQLRRF
    160 170 180 190 200
    AHNDVTHLAR LLASPCPGQQ MVVTEGVFSM DGDSAPLAEI QQVTQQHNGW
    210 220 230 240 250
    LMVDDAHGTG VIGEQGRGSC WLQKVKPELL VVTFGKGFGV SGAAVLCSST
    260 270 280 290 300
    VADYLLQFAR HLIYSTSMPP AQAQALRASL AVIRSDEGDA RREKLAALIT
    310 320 330 340 350
    RFRAGVQDLP FTLADSCSAI QPLIVGDNSR ALQLAEKLRQ QGCWVTAIRP
    360 370 380
    PTVPAGTARL RLTLTAAHEM QDIDRLLEVL HGNG
    Length:384
    Mass (Da):41,594
    Last modified:January 1, 1990 - v1
    Checksum:iD1AF5C054A5B4B06
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti188 – 189AE → R in CAA00968 (Ref. 2) Curated2

    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:
    EMBLi
    GenBanki
    DDBJi
    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.
    WP_000118826.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73863; AAC73863; b0776.
    BAE76363; BAE76363; BAE76363.
    GeneIDi945384.
    KEGGiecj:JW0759.
    eco:b0776.
    PATRICi32116753. VBIEscCol129921_0802.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.
    WP_000118826.1. NZ_LN832404.1.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi4259953. 17 interactors.
    DIPiDIP-6870N.
    IntActiP12998. 2 interactors.
    STRINGi511145.b0776.

    Proteomic databases

    PaxDbiP12998.
    PRIDEiP12998.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73863; AAC73863; b0776.
    BAE76363; BAE76363; BAE76363.
    GeneIDi945384.
    KEGGiecj:JW0759.
    eco:b0776.
    PATRICi32116753. VBIEscCol129921_0802.

    Organism-specific databases

    EchoBASEiEB0119.
    EcoGeneiEG10121. bioF.

    Phylogenomic databases

    eggNOGiENOG4107EEK. Bacteria.
    COG0156. LUCA.
    HOGENOMiHOG000221021.
    InParanoidiP12998.
    KOiK00652.
    OMAiELAHACI.
    PhylomeDBiP12998.

    Enzyme and pathway databases

    UniPathwayiUPA00078.
    BioCyciEcoCyc:7KAPSYN-MONOMER.
    ECOL316407:JW0759-MONOMER.
    MetaCyc:7KAPSYN-MONOMER.
    BRENDAi2.3.1.47. 2026.
    SABIO-RKP12998.

    Miscellaneous databases

    EvolutionaryTraceiP12998.
    PROiP12998.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01693. BioF_aminotrans_2. 1 hit.
    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]
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 145 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

    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 one 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.