Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P12998 (BIOF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
8-amino-7-oxononanoate synthase

Short name=AONS
EC=2.3.1.47
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 names
Name:bioF
Ordered Locus Names:b0776, JW0759
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Catalytic activity

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

Cofactor

Pyridoxal phosphate. Ref.5

Enzyme regulation

Competitively inhibited by D-alanine, 8-amino-7-hydroxy-8-phosphonononanoic acid and 2-amino-3-hydroxy-2-methylnonadioic acid. Ref.6

Pathway

Cofactor biosynthesis; biotin biosynthesis. HAMAP-Rule MF_01693

Subunit structure

Homodimer. Ref.8

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=25 µM for pimeloyl-CoA (at pH 7.5 and at 30 degrees Celsius) Ref.5

KM=0.5 µM for L-alanine (at pH 7.5 and at 30 degrees Celsius)

Mass spectrometry

Molecular mass is 41464.4±4.5 Da from positions 2 - 384. Determined by ESI. Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 3843838-amino-7-oxononanoate synthase HAMAP-Rule MF_01693
PRO_0000163811

Regions

Region108 – 1092Pyridoxal phosphate binding HAMAP-Rule MF_01693
Region204 – 2074Pyridoxal phosphate binding HAMAP-Rule MF_01693
Region233 – 2364Pyridoxal phosphate binding HAMAP-Rule MF_01693

Sites

Binding site211Substrate
Binding site1331Substrate
Binding site1791Pyridoxal phosphate
Binding site3521Substrate

Amino acid modifications

Modified residue2361N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_01693

Experimental info

Sequence conflict188 – 1892AE → R in CAA00968. Ref.2

Secondary structure

..................................................................... 384
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12998 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: D1AF5C054A5B4B06

FASTA38441,594
        10         20         30         40         50         60 
MSWQEKINAA LDARRAADAL RRRYPVAQGA GRWLVADDRQ YLNFSSNDYL GLSHHPQIIR 

        70         80         90        100        110        120 
AWQQGAEQFG IGSGGSGHVS GYSVVHQALE EELAEWLGYS RALLFISGFA ANQAVIAAMM 

       130        140        150        160        170        180 
AKEDRIAADR LSHASLLEAA SLSPSQLRRF AHNDVTHLAR LLASPCPGQQ MVVTEGVFSM 

       190        200        210        220        230        240 
DGDSAPLAEI QQVTQQHNGW LMVDDAHGTG VIGEQGRGSC WLQKVKPELL VVTFGKGFGV 

       250        260        270        280        290        300 
SGAAVLCSST VADYLLQFAR HLIYSTSMPP AQAQALRASL AVIRSDEGDA RREKLAALIT 

       310        320        330        340        350        360 
RFRAGVQDLP FTLADSCSAI QPLIVGDNSR ALQLAEKLRQ QGCWVTAIRP PTVPAGTARL 

       370        380 
RLTLTAAHEM QDIDRLLEVL HGNG 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04423 Genomic DNA. Translation: AAA23516.1.
A11542 Unassigned DNA. Translation: CAA00968.1.
U00096 Genomic DNA. Translation: AAC73863.1.
AP009048 Genomic DNA. Translation: BAE76363.1.
PIRSYECKP. D32025.
RefSeqNP_415297.1. NC_000913.3.
YP_489049.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BS0X-ray1.65A1-384[»]
1DJ9X-ray2.00A1-384[»]
1DJEX-ray1.71A1-384[»]
2G6WX-ray2.14A1-384[»]
ProteinModelPortalP12998.
SMRP12998. Positions 2-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6870N.
IntActP12998. 2 interactions.
STRING511145.b0776.

Proteomic databases

PaxDbP12998.
PRIDEP12998.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73863; AAC73863; b0776.
BAE76363; BAE76363; BAE76363.
GeneID12930959.
945384.
KEGGecj:Y75_p0749.
eco:b0776.
PATRIC32116753. VBIEscCol129921_0802.

Organism-specific databases

EchoBASEEB0119.
EcoGeneEG10121. bioF.

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000221021.
KOK00652.
OMARICLHAF.
OrthoDBEOG6Q8HZD.
PhylomeDBP12998.

Enzyme and pathway databases

BioCycEcoCyc:7KAPSYN-MONOMER.
ECOL316407:JW0759-MONOMER.
MetaCyc:7KAPSYN-MONOMER.
UniPathwayUPA00078.

Gene expression databases

GenevestigatorP12998.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01693. BioF_aminotrans_2.
InterProIPR022834. Amino_oxononanoate_synth.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR004723. BioF.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00858. bioF. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12998.
PROP12998.

Entry information

Entry nameBIOF_ECOLI
AccessionPrimary (citable) accession number: P12998
Secondary accession number(s): Q2MBJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 14, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene