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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)DescriptionActionsGraphical viewLength
Active sitei2531
Active sitei2891

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi229 – 234NADP6

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000564661 – 510NADP-dependent fatty aldehyde dehydrogenaseAdd BLAST510

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1510
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 12Combined sources5
Turni14 – 16Combined sources3
Beta strandi17 – 19Combined sources3
Helixi29 – 48Combined sources20
Helixi51 – 67Combined sources17
Helixi69 – 80Combined sources12
Helixi84 – 107Combined sources24
Helixi109 – 111Combined sources3
Beta strandi113 – 116Combined sources4
Beta strandi123 – 125Combined sources3
Beta strandi130 – 136Combined sources7
Beta strandi140 – 143Combined sources4
Beta strandi146 – 148Combined sources3
Turni149 – 152Combined sources4
Helixi157 – 165Combined sources9
Beta strandi169 – 172Combined sources4
Helixi178 – 195Combined sources18
Helixi199 – 201Combined sources3
Beta strandi202 – 205Combined sources4
Helixi211 – 218Combined sources8
Beta strandi224 – 229Combined sources6
Helixi231 – 243Combined sources13
Beta strandi244 – 246Combined sources3
Beta strandi250 – 253Combined sources4
Beta strandi259 – 262Combined sources4
Helixi264 – 269Combined sources6
Helixi273 – 281Combined sources9
Helixi283 – 286Combined sources4
Beta strandi294 – 300Combined sources7
Helixi301 – 316Combined sources16
Helixi325 – 339Combined sources15
Beta strandi344 – 348Combined sources5
Beta strandi359 – 364Combined sources6
Helixi365 – 370Combined sources6
Helixi372 – 375Combined sources4
Beta strandi380 – 390Combined sources11
Helixi391 – 399Combined sources9
Beta strandi404 – 410Combined sources7
Helixi413 – 415Combined sources3
Helixi416 – 427Combined sources12
Beta strandi430 – 437Combined sources8
Beta strandi445 – 447Combined sources3
Beta strandi460 – 462Combined sources3
Beta strandi464 – 466Combined sources3
Helixi467 – 473Combined sources7
Beta strandi474 – 481Combined sources8
Helixi484 – 486Combined sources3
Helixi489 – 491Combined sources3
Beta strandi501 – 503Combined sources3

3D structure databases

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

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: November 2, 2016
This is version 88 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.