U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

BIO3 adenosylmethionine-8-amino-7-oxononanoate transaminase [ Saccharomyces cerevisiae S288C ]

Gene ID: 855795, updated on 2-Nov-2024

Summary

Official Symbol
BIO3
Official Full Name
adenosylmethionine-8-amino-7-oxononanoate transaminase
Primary source
SGD:S000005341
Locus tag
YNR058W
See related
AllianceGenome:SGD:S000005341; FungiDB:YNR058W; VEuPathDB:YNR058W
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables adenosylmethionine-8-amino-7-oxononanoate transaminase activity. Involved in biotin biosynthetic process. Predicted to be located in cytoplasm. Predicted to be active in mitochondrion. [provided by Alliance of Genome Resources, Nov 2024]
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

See BIO3 in Genome Data Viewer
Location:
chromosome: XIV
Exon count:
1
Sequence:
Chromosome: XIV; NC_001146.8 (734291..735733)

Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene Bio5p Neighboring gene dethiobiotin synthase Neighboring gene putative alpha-1,3-mannosyltransferase Neighboring gene ferric-chelate reductase

Bibliography

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables adenosylmethionine-8-amino-7-oxononanoate transaminase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables adenosylmethionine-8-amino-7-oxononanoate transaminase activity IDA
Inferred from Direct Assay
more info
PubMed 
enables adenosylmethionine-8-amino-7-oxononanoate transaminase activity IEA
Inferred from Electronic Annotation
more info
 
enables dethiobiotin synthase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables pyridoxal phosphate binding IEA
Inferred from Electronic Annotation
more info
 
enables transaminase activity IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
involved_in biotin biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in biotin biosynthetic process IDA
Inferred from Direct Assay
more info
PubMed 
involved_in biotin biosynthetic process IEA
Inferred from Electronic Annotation
more info
 
involved_in biotin biosynthetic process IMP
Inferred from Mutant Phenotype
more info
PubMed 
Component Evidence Code Pubs
located_in cytoplasm ISS
Inferred from Sequence or Structural Similarity
more info
PubMed 
is_active_in mitochondrion IBA
Inferred from Biological aspect of Ancestor
more info
 

General protein information

Preferred Names
adenosylmethionine-8-amino-7-oxononanoate transaminase
NP_014456.1
  • 7,8-diamino-pelargonic acid aminotransferase (DAPA); catalyzes the second step in the biotin biosynthesis pathway; BIO3 is in a cluster of 3 genes (BIO3, BIO4, and BIO5) that mediate biotin synthesis; BIO3 and BIO4 were acquired by horizontal gene transfer (HGT) from bacteria

NCBI Reference Sequences (RefSeq)

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001146.8 Reference assembly

    Range
    734291..735733
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001183235.1NP_014456.1  TPA: adenosylmethionine-8-amino-7-oxononanoate transaminase [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_014456.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W1N3, E9P967, P50277, Q4R1J0
    UniProtKB/TrEMBL
    A6ZSD2, B3LPI5, C7GIY7, C8ZFT7
    Conserved Domains (1) summary
    cl18945
    Location:15472
    AAT_I; Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the ...