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B0UKC8 (BIOF_METS4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Alpha-oxoamine synthase
Gene names
Ordered Locus Names:M446_5168
OrganismMethylobacterium sp. (strain 4-46) [Complete proteome] [HAMAP]
Taxonomic identifier426117 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Cofactor biosynthesis; biotin biosynthesis.

Subunit structure

Homodimer By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processBiotin biosynthesis
   LigandPyridoxal phosphate
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processbiotin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_function8-amino-7-oxononanoate synthase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3793798-amino-7-oxononanoate synthase
PRO_0000381029

Regions

Region114 – 1152Pyridoxal phosphate binding By similarity
Region212 – 2154Pyridoxal phosphate binding By similarity
Region232 – 2354Pyridoxal phosphate binding By similarity

Sites

Binding site271Substrate By similarity
Binding site341Substrate By similarity
Binding site1391Substrate By similarity
Binding site1871Pyridoxal phosphate By similarity
Binding site3441Substrate By similarity

Amino acid modifications

Modified residue2351N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0UKC8 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 3700381E5CD27219

FASTA37939,067
        10         20         30         40         50         60 
MPVPPTLSLD AFAAAKLAGL DAAGLRRRLV PTARTGGARA ERDGRAVVSF SCNDYLGLAT 

        70         80         90        100        110        120 
HPEVVAAAHA ALDRYGAGSG GSRLVTGSHP ILAELEAALA ARKGHEAALV FGSGYLANLG 

       130        140        150        160        170        180 
VTPALVGAGD LILIDELGHS CMWAGTRLAG ARALPFRHND LGHLEDLLAR ERARARRALI 

       190        200        210        220        230        240 
LTERVFSMDG DRAPVAEILG LARAFDAWTL VDDAHGLGVV GPDATAPLEM GTLSKALGSY 

       250        260        270        280        290        300 
GGYLCASRPV IDLLTSRARS FVYTTGLPPA SAAAALAALR LIEAEPARAA RPLALARRFT 

       310        320        330        340        350        360 
ARLGLPEAQS AVVPVLVGEA EAALALSRAL EARGFLVVAI RPPTVPPGTA RLRVAFSAAH 

       370 
EEAEVDALAQ ALLDLGAAA

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium sp. 4-46."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ivanova N., Marx C.J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 4-46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000943 Genomic DNA. Translation: ACA19493.1.
RefSeqYP_001771927.1. NC_010511.1.

3D structure databases

ProteinModelPortalB0UKC8.
ModBaseSearch...

Protein-protein interaction databases

STRING426117.M446_5168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA19493; ACA19493; M446_5168.
GeneID6133428.
KEGGmet:M446_5168.
PATRIC22591526. VBIMetSp32184_5083.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000221021.
KOK00652.
OMAQRAPLEM.
ProtClustDBCLSK890485.

Enzyme and pathway databases

BioCycMSP426117:GI2I-5223-MONOMER.
UniPathwayUPA00078.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
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. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBIOF_METS4
AccessionPrimary (citable) accession number: B0UKC8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 8, 2008
Last modified: May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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