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Reviewed, UniProtKB/Swiss-Prot P56533 (BADH_GADCA)

Last modified November 4, 2008. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 callarias (Baltic cod)
Taxonomic identifier8053 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiNeoteleosteiAcanthomorphaParacanthopterygiiGadiformesGadidaeGadus

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Betaine aldehyde + NAD(+) + H(2)O = betaine + NADH.

An aldehyde + NAD(+) + H(2)O = an acid + NADH.

Pathway

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

Subunit structure

Homotetramer.

Subcellular location

CytoplasmBy similarity.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords

   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionaldehyde dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

betaine-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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P56533-1 [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: 9792097] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Tissue: Liver.

Cross-references

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1A4SX-ray2.10A/B/C/D1-503[»]
1BPWX-ray2.80A/B/C/D1-503[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2908N.

Phylogenomic databases

HOVERGENP56533.

Family and domain databases

InterProIPR016160. Ald_DHase_CS.
IPR016162. Ald_DHase_N.
IPR015590. Aldehyde_DHase.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP56533.

Entry information

Entry nameBADH_GADCA
AccessionPrimary (citable) accession number: P56533
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 4, 2008
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents