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Protein

NADP-dependent fatty aldehyde dehydrogenase

Gene

aldH

Organism
Vibrio harveyi (Beneckea harveyi)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

An aldehyde + NADP+ + H2O = a carboxylate + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei253 – 2531
Active sitei289 – 2891

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi229 – 2346NADP

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NADP-dependent fatty aldehyde dehydrogenase (EC:1.2.1.4)
Gene namesi
Name:aldH
OrganismiVibrio harveyi (Beneckea harveyi)
Taxonomic identifieri669 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 510510NADP-dependent fatty aldehyde dehydrogenasePRO_0000056466Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
510
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Turni14 – 163Combined sources
Beta strandi17 – 193Combined sources
Helixi29 – 4820Combined sources
Helixi51 – 6717Combined sources
Helixi69 – 8012Combined sources
Helixi84 – 10724Combined sources
Helixi109 – 1113Combined sources
Beta strandi113 – 1164Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi130 – 1367Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi146 – 1483Combined sources
Turni149 – 1524Combined sources
Helixi157 – 1659Combined sources
Beta strandi169 – 1724Combined sources
Helixi178 – 19518Combined sources
Helixi199 – 2013Combined sources
Beta strandi202 – 2054Combined sources
Helixi211 – 2188Combined sources
Beta strandi224 – 2296Combined sources
Helixi231 – 24313Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi250 – 2534Combined sources
Beta strandi259 – 2624Combined sources
Helixi264 – 2696Combined sources
Helixi273 – 2819Combined sources
Helixi283 – 2864Combined sources
Beta strandi294 – 3007Combined sources
Helixi301 – 31616Combined sources
Helixi325 – 33915Combined sources
Beta strandi344 – 3485Combined sources
Beta strandi359 – 3646Combined sources
Helixi365 – 3706Combined sources
Helixi372 – 3754Combined sources
Beta strandi380 – 39011Combined sources
Helixi391 – 3999Combined sources
Beta strandi404 – 4107Combined sources
Helixi413 – 4153Combined sources
Helixi416 – 42712Combined sources
Beta strandi430 – 4378Combined sources
Beta strandi445 – 4473Combined sources
Beta strandi460 – 4623Combined sources
Beta strandi464 – 4663Combined sources
Helixi467 – 4737Combined sources
Beta strandi474 – 4818Combined sources
Helixi484 – 4863Combined sources
Helixi489 – 4913Combined sources
Beta strandi501 – 5033Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EYYX-ray2.50A/B/C/D1-510[»]
1EZ0X-ray2.10A/B/C/D1-510[»]
ProteinModelPortaliQ56694.
SMRiQ56694. Positions 5-508.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ56694.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.

Sequencei

Sequence statusi: Complete.

Q56694-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPQTDNVFY ATNAFTGEAL PLAFPVHTEV EVNQAATAAA KVARDFRRLN
60 70 80 90 100
NSKRASLLRT IASELEARSD DIIARAHLET ALPEVRLTGE IARTANQLRL
110 120 130 140 150
FADVVNSGSY HQAILDTPNP TRAPLPKPDI RRQQIALGPV AVFGASNFPL
160 170 180 190 200
AFSAAGGDTA SALAAGCPVI VKGHTAHPGT SQIVAECIEQ ALKQEQLPQA
210 220 230 240 250
IFTLLQGNQR ALGQALVSHP EIKAVGFTGS VGGGRALFNL AHERPEPIPF
260 270 280 290 300
YGELGAINPT FIFPSAMRAK ADLADQFVAS MTMGCGQFCT KPGVVFALNT
310 320 330 340 350
PETQAFIETA QSLIRQQSPS TLLTPGIRDS YQSQVVSRGS DDGIDVTFSQ
360 370 380 390 400
AESPCVASAL FVTSSENWRK HPAWEEEIFG PQSLIVVCEN VADMLSLSEM
410 420 430 440 450
LAGSLTATIH ATEEDYPQVS QLIPRLEEIA GRLVFNGWPT GVEVGYAMVH
460 470 480 490 500
GGPYPASTHS ASTSVGAEAI HRWLRPVAYQ ALPESLLPDS LKAENPLEIA
510
RAVDGKAAHS
Length:510
Mass (Da):54,460
Last modified:November 1, 1996 - v1
Checksum:iE132F2406AA3F47A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39638 Genomic DNA. Translation: AAA89078.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39638 Genomic DNA. Translation: AAA89078.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EYYX-ray2.50A/B/C/D1-510[»]
1EZ0X-ray2.10A/B/C/D1-510[»]
ProteinModelPortaliQ56694.
SMRiQ56694. Positions 5-508.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ56694.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    Strain: ATCC 33843 / 392 / MAV.

Entry informationi

Entry nameiALDH_VIBHA
AccessioniPrimary (citable) accession number: Q56694
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1996
Last modified: October 14, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.