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Reviewed, UniProtKB/Swiss-Prot Q56694 (ALDH_VIBHA)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    NADP-dependent fatty aldehyde dehydrogenase
    EC=1.2.1.4
Gene names
Name: aldH
OrganismVibrio harveyi
Taxonomic identifier669 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

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Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the oxidation of long-chain aliphatic aldehydes to acids. May be implicated in controlling luminescence as it catalyzes the oxidation of the fatty aldehyde substrate for the light-emitting reaction.

Catalytic activity

An aldehyde + NADP+ + H2O = an acid + NADPH.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

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Ontologies

Keywords
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionaldehyde dehydrogenase (NADP+) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510NADP-dependent fatty aldehyde dehydrogenase
PRO_0000056466

Regions

Nucleotide binding229 – 2346NADP

Sites

Active site2531
Active site2891

Secondary structure

1 .................................................................................... 510
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q56694-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E132F2406AA3F47A

FASTA51054,460
        10         20         30         40         50         60 
MNPQTDNVFY ATNAFTGEAL PLAFPVHTEV EVNQAATAAA KVARDFRRLN NSKRASLLRT 

        70         80         90        100        110        120 
IASELEARSD DIIARAHLET ALPEVRLTGE IARTANQLRL FADVVNSGSY HQAILDTPNP 

       130        140        150        160        170        180 
TRAPLPKPDI RRQQIALGPV AVFGASNFPL AFSAAGGDTA SALAAGCPVI VKGHTAHPGT 

       190        200        210        220        230        240 
SQIVAECIEQ ALKQEQLPQA IFTLLQGNQR ALGQALVSHP EIKAVGFTGS VGGGRALFNL 

       250        260        270        280        290        300 
AHERPEPIPF YGELGAINPT FIFPSAMRAK ADLADQFVAS MTMGCGQFCT KPGVVFALNT 

       310        320        330        340        350        360 
PETQAFIETA QSLIRQQSPS TLLTPGIRDS YQSQVVSRGS DDGIDVTFSQ AESPCVASAL 

       370        380        390        400        410        420 
FVTSSENWRK HPAWEEEIFG PQSLIVVCEN VADMLSLSEM LAGSLTATIH ATEEDYPQVS 

       430        440        450        460        470        480 
QLIPRLEEIA GRLVFNGWPT GVEVGYAMVH GGPYPASTHS ASTSVGAEAI HRWLRPVAYQ 

       490        500        510 
ALPESLLPDS LKAENPLEIA RAVDGKAAHS

« Hide

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References

[1]"Involvement of cysteine 289 in the catalytic activity of an NADP(+)-specific fatty aldehyde dehydrogenase from Vibrio harveyi."
Vedadi M., Szittner R., Smillie L., Meighen E.
Biochemistry 34:16725-16732(1995) [PubMed: 8527447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
Strain: ATCC 33843 / 392 / MAV.
[2]"Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity."
Ahvazi B., Coulombe R., Delarge M., Vedadi M., Zhang L., Meighen E., Vrielink A.
Biochem. J. 349:853-861(2000) [PubMed: 10903148] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Strain: ATCC 33843 / 392 / MAV.

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Cross-references

Sequence databases

U39638 Genomic DNA. Translation: AAA89078.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1EYYX-ray2.50A/B/C/D1-510[»]
1EZ0X-ray2.10A/B/C/D1-510[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.4. 351.

Family and domain databases

InterProIPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
[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. False negative.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameALDH_VIBHA
AccessionPrimary (citable) accession number: Q56694
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

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