NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
STRAIN=ATCC 33843 / 392 / MAV;
DOI=10.1021/bi00051a022; PubMed=8527447 [NCBI, ExPASy, EBI, Israel, Japan]
Vedadi M., Szittner R., Smillie L., Meighen E.;
"Involvement of cysteine 289 in the catalytic activity of an NADP(+)-specific fatty aldehyde dehydrogenase from Vibrio harveyi.";
Biochemistry 34:16725-16732(1995).

[2]

X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
STRAIN=ATCC 33843 / 392 / MAV;
PubMed=10903148 [NCBI, ExPASy, EBI, Israel, Japan]
Ahvazi B., Coulombe R., Delarge M., Vedadi M., Zhang L., Meighen E., Vrielink A.;
"Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity.";
Biochem. J. 349:853-861(2000).

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: Homodimer.
SIMILARITY: Belongs to the aldehyde dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U39638; AAA89078.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1EYY; X-ray; 2.50 A; A/B/C/D=1-510.	[ExPASy / RCSB / EBI]
1EZ0; X-ray; 2.10 A; A/B/C/D=1-510.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1EYY; -.
1EZ0; -.

ModBase

Q56694.

Ontologies

GO:0033721;	Molecular function: aldehyde dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; FALSE_NEG.
PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 510`	`510`	`NADP-dependent fatty aldehyde dehydrogenase.`	`PRO_0000056466`
`NP_BIND`	`229 234`	`6`	`NADP.`
`ACT_SITE`	`253 253`
`ACT_SITE`	`289 289`
`TURN`	`14 16`	`3`
`STRAND`	`17 19`	`3`
`HELIX`	`29 48`	`20`
`HELIX`	`51 67`	`17`
`HELIX`	`69 80`	`12`
`HELIX`	`84 107`	`24`
`HELIX`	`109 111`	`3`
`STRAND`	`113 116`	`4`
`STRAND`	`123 125`	`3`
`STRAND`	`130 136`	`7`
`STRAND`	`140 143`	`4`
`TURN`	`149 152`	`4`
`HELIX`	`157 165`	`9`
`STRAND`	`169 172`	`4`
`HELIX`	`178 195`	`18`
`HELIX`	`199 201`	`3`
`STRAND`	`202 205`	`4`
`HELIX`	`211 218`	`8`
`STRAND`	`224 229`	`6`
`HELIX`	`231 243`	`13`
`STRAND`	`244 246`	`3`
`STRAND`	`250 253`	`4`
`STRAND`	`259 262`	`4`
`HELIX`	`264 269`	`6`
`HELIX`	`273 281`	`9`
`HELIX`	`283 286`	`4`
`STRAND`	`294 300`	`7`
`HELIX`	`301 316`	`16`
`HELIX`	`325 339`	`15`
`STRAND`	`344 348`	`5`
`STRAND`	`359 364`	`6`
`HELIX`	`365 370`	`6`
`HELIX`	`372 375`	`4`
`STRAND`	`380 390`	`11`
`HELIX`	`391 399`	`9`
`STRAND`	`404 410`	`7`
`HELIX`	`413 415`	`3`
`HELIX`	`416 427`	`12`
`STRAND`	`430 437`	`8`
`STRAND`	`445 447`	`3`
`STRAND`	`464 466`	`3`
`HELIX`	`467 473`	`7`
`STRAND`	`474 481`	`8`
`HELIX`	`484 486`	`3`
`HELIX`	`489 491`	`3`
`STRAND`	`501 503`	`3`

Sequence information

Length: 510 AA [This is the length of the unprocessed precursor]

Molecular weight: 54460 Da [This is the MW of the unprocessed precursor]

CRC64: E132F2406AA3F47A [This is a checksum on the sequence]

        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

Q56694 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools