Q802W2 · A9A1B_DANRE

Function

function

Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine with high efficiency (in vitro). Can catalyze the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction, but with low efficiency.

Catalytic activity

Pathway

Amine and polyamine biosynthesis; carnitine biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site204NAD+ (UniProtKB | ChEBI)
Binding site256-260NAD+ (UniProtKB | ChEBI)
Active site278Proton acceptor
Active site312Nucleophile
Binding site415NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function4-trimethylammoniobutyraldehyde dehydrogenase activity
Molecular Functionaminobutyraldehyde dehydrogenase (NAD+) activity
Biological Processcarnitine biosynthetic process
Biological Processcellular aldehyde metabolic process
Biological Processprotein homotetramerization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    4-trimethylaminobutyraldehyde dehydrogenase B
  • EC number
  • Short names
    TMABA-DH; TMABADH
  • Alternative names
    • Aldehyde dehydrogenase family 9 member A1-B (EC:1.2.1.3
      ) . EC:1.2.1.3 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      aldh9a1b
    • Synonyms
      aldh9a1
    • ORF names
      si:ch211-284b7.5

Organism names

  • Taxonomic identifier
  • Strains
    • Tuebingen
    • AB
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    Q802W2
  • Secondary accessions
    • A2AWD6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003006251-5184-trimethylaminobutyraldehyde dehydrogenase B

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    518
  • Mass (Da)
    56,438
  • Last updated
    2007-10-23 v2
  • Checksum
    105AB1667E4199FF
MALMRCLLPPGFYRTLYHPWTRCASSGTLQIKDPLNFWCGARVDLKDVKTKSEPVFEPATGRVLCRLQTCGSAEVDAAVRNASAAFKVWRKLSGMERARVMLEAARLIEKRREEIAEMEVINNGKSITEARLDVDSARLSIEYFAGQATTLSGQHVQLPGGSFAYTRREPFGVCVGIGAWNYPFQIAAWKSAPAIACGNSMVFKPSPLTPVTAVLLAEIYRQAGAPEGLFNVVQGGQETGSLLCLHPSVEKVSFTGSVPTGKKIMEMASRGVKAVTLELGGKSPLIIFEDTDLENAVRGALMANFLSQGQVCSNGTRVFVQSSIVPQFLKEVVRRTKAISIGDPLLDETRMGALVSKAHLDKVLRYVEQAKNEGAQVLCGGEPFSPADPKLKDGYYMTPCVLDSCTDDMTCVKEEIFGPVMSVLTFDTEDEVLRRANDSDLGLAAGVFTKDVKRAHRVIENLQAGSCFINNYNITPVEVPFGGFKASGIGRENGQVTIEFYSQLKTVVVEMGDVDSLF

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8M3AVP0A0A8M3AVP0_DANREaldh9a1b539

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict18-20in Ref. 2; AAH47176
Sequence conflict84in Ref. 2; AAH47176
Sequence conflict87in Ref. 2; AAH47176
Sequence conflict102in Ref. 2; AAH47176
Sequence conflict140in Ref. 2; AAH47176
Sequence conflict167in Ref. 2; AAH47176
Sequence conflict227in Ref. 2; AAH47176
Sequence conflict342in Ref. 2; AAH47176

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL954171
EMBL· GenBank· DDBJ
CAM14219.1
EMBL· GenBank· DDBJ
Genomic DNA
BC047176
EMBL· GenBank· DDBJ
AAH47176.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp