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P56533 (BADH_GADMC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Betaine aldehyde dehydrogenase
Short name=BADH
EC=1.2.1.8
Alternative name(s):
Aldehyde dehydrogenase family 9 member A1
EC=1.2.1.3
Gene names
Name:aldh9A1
OrganismGadus morhua subsp. callarias (Baltic cod) (Gadus callarias)
Taxonomic identifier8053 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Paracanthopterygii › Gadiformes › Gadidae › Gadus ›

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Betaine aldehyde + NAD+ + H2O = betaine + NADH.

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Pathway

Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processglycine betaine biosynthetic process from choline

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbetaine-aldehyde dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503Betaine aldehyde dehydrogenase
PRO_0000056532

Regions

Nucleotide binding241 – 2466NAD By similarity

Sites

Active site2631Proton acceptor
Active site2971Nucleophile
Site1661Transition state stabilizer

Secondary structure

1 ........................................................................................ 503
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56533 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 1CB2FB92FA89E577

FASTA50354,368
        10         20         30         40         50         60 
AQLVDSMPSA STGSVVVTDD LNYWGGRRIK SKDGATTEPV FEPATGRVLC QMVPCGAEEV 

        70         80         90        100        110        120 
DQAVQSAQAA YLKWSKMAGI ERSRVMLEAA RIIRERRDNI AKLEVINNGK TITEAEYDID 

       130        140        150        160        170        180 
AAWQCIEYYA GLAPTLSGQH IQLPGGAFAY TRREPLGVCA GILAWNYPFM IAAWKCAPAL 

       190        200        210        220        230        240 
ACGNAVVFKP SPMTPVTGVI LAEIFHEAGV PVGLVNVVQG GAETGSLLCH HPNVAKVSFT 

       250        260        270        280        290        300 
GSVPTGKKVM EMSAKTVKHV TLELGGKSPL LIFKDCELEN AVRGALMANF LTQGQVCTNG 

       310        320        330        340        350        360 
TRVFVQREIM PQFLEEVVKR TKAIVVGDPL LTETRMGGLI SKPQLDKVLG FVAQAKKEGA 

       370        380        390        400        410        420 
RVLCGGEPLT PSDPKLKNGY FMSPCVLDNC RDDMTCVKEE IFGPVMSVLP FDTEEEVLQR 

       430        440        450        460        470        480 
ANNTTFGLAS GVFTRDISRA HRVAANLEAG TCYINTYSIS PVEVPFGGYK MSGFGRENGQ 

       490        500 
ATVDYYSQLK TVIVEMGDVD SLF

« Hide

References

[1]"Structure of betaine aldehyde dehydrogenase at 2.1-A resolution."
Johansson K., El-Ahmad M., Ramaswamy S., Hjelmqvist L., Joernvall H., Eklund H.
Protein Sci. 7:2106-2117(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Tissue: Liver.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4SX-ray2.10A/B/C/D1-503[»]
1BPWX-ray2.80A/B/C/D1-503[»]
ProteinModelPortalP56533.
SMRP56533. Positions 1-503.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2908N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000097.

Enzyme and pathway databases

UniPathwayUPA00529; UER00386.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP56533.

Entry information

Entry nameBADH_GADMC
AccessionPrimary (citable) accession number: P56533
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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