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Protein

Aldehyde dehydrogenase, mitochondrial

Gene

ALDH2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Pathwayi: ethanol degradation

This protein is involved in step 2 of the subpathway that synthesizes acetate from ethanol.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Aldehyde dehydrogenase X, mitochondrial (ALDH1B1), Aldehyde dehydrogenase, mitochondrial (ALDH2), Aldehyde dehydrogenase family 3 member B1 (ALDH3B1)
This subpathway is part of the pathway ethanol degradation, which is itself part of Alcohol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetate from ethanol, the pathway ethanol degradation and in Alcohol metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei189Transition state stabilizer1 Publication1
Active sitei288Proton acceptor1
Active sitei322Nucleophile1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi265 – 270NADBy similarity6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-BTA-380612. Metabolism of serotonin.
R-BTA-71384. Ethanol oxidation.
SABIO-RKP20000.
UniPathwayiUPA00780; UER00768.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase, mitochondrial (EC:1.2.1.3)
Alternative name(s):
ALDH class 2
ALDH-E2
ALDHI
Gene namesi
Name:ALDH2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 17

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 21Mitochondrion1 PublicationAdd BLAST21
ChainiPRO_000000716722 – 520Aldehyde dehydrogenase, mitochondrialAdd BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei55N6-acetyllysineBy similarity1
Modified residuei76N6-acetyllysineBy similarity1
Modified residuei162N6-acetyllysineBy similarity1
Modified residuei371N6-acetyllysineBy similarity1
Modified residuei378N6-acetyllysineBy similarity1
Modified residuei386N6-acetyllysineBy similarity1
Modified residuei429N6-acetyllysineBy similarity1
Modified residuei431N6-acetyllysineBy similarity1
Modified residuei444N6-acetyllysineBy similarity1
Modified residuei454N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP20000.
PeptideAtlasiP20000.
PRIDEiP20000.

Expressioni

Gene expression databases

BgeeiENSBTAG00000008743.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000011521.

Structurei

Secondary structure

1520
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 46Combined sources6
Beta strandi47 – 49Combined sources3
Beta strandi56 – 60Combined sources5
Turni62 – 64Combined sources3
Beta strandi67 – 72Combined sources6
Helixi76 – 89Combined sources14
Helixi95 – 98Combined sources4
Helixi101 – 117Combined sources17
Helixi119 – 130Combined sources12
Helixi134 – 139Combined sources6
Helixi141 – 153Combined sources13
Turni154 – 158Combined sources5
Beta strandi161 – 164Combined sources4
Beta strandi167 – 178Combined sources12
Beta strandi181 – 185Combined sources5
Beta strandi188 – 190Combined sources3
Helixi191 – 205Combined sources15
Beta strandi208 – 213Combined sources6
Helixi219 – 231Combined sources13
Beta strandi237 – 243Combined sources7
Helixi245 – 253Combined sources9
Beta strandi260 – 265Combined sources6
Helixi267 – 279Combined sources13
Beta strandi284 – 288Combined sources5
Beta strandi294 – 297Combined sources4
Helixi303 – 315Combined sources13
Helixi316 – 319Combined sources4
Beta strandi327 – 331Combined sources5
Helixi332 – 348Combined sources17
Helixi367 – 383Combined sources17
Beta strandi386 – 389Combined sources4
Beta strandi392 – 394Combined sources3
Beta strandi396 – 398Combined sources3
Beta strandi404 – 408Combined sources5
Helixi414 – 417Combined sources4
Beta strandi422 – 430Combined sources9
Helixi433 – 441Combined sources9
Beta strandi447 – 452Combined sources6
Helixi456 – 465Combined sources10
Beta strandi469 – 474Combined sources6
Beta strandi492 – 494Combined sources3
Helixi500 – 503Combined sources4
Beta strandi506 – 514Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A4ZX-ray2.75A/B/C/D22-520[»]
1AG8X-ray2.65A/B/C/D22-520[»]
ProteinModelPortaliP20000.
SMRiP20000.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20000.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP20000.
KOiK00128.
OMAiTIACGGE.
OrthoDBiEOG091G05E8.
TreeFamiTF300455.

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.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20000-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRAVALAAA RLGPRQGRRL LSAATQAVPT PNQQPEVLYN QIFINNEWHD
60 70 80 90 100
AVSKKTFPTV NPSTGDVICH VAEGDKADVD RAVKAARAAF QLGSPWRRMD
110 120 130 140 150
ASERGRLLNR LADLIERDRT YLAALETLDN GKPYIISYLV DLDMVLKCLR
160 170 180 190 200
YYAGWADKYH GKTIPIDGDY FSYTRHEPVG VCGQIIPWNF PLLMQAWKLG
210 220 230 240 250
PALATGNVVV MKVAEQTPLT ALYVANLIKE AGFPPGVVNV IPGFGPTAGA
260 270 280 290 300
AIASHEDVDK VAFTGSTEVG HLIQVAAGKS NLKRVTLELG GKSPNIIMSD
310 320 330 340 350
ADMDWAVEQA HFALFFNQGQ CCCAGSRTFV QEDIYAEFVE RSVARAKSRV
360 370 380 390 400
VGNPFDSRTE QGPQVDETQF KKVLGYIKSG KEEGAKLLCG GGAAADRGYF
410 420 430 440 450
IQPTVFGDVQ DGMTIAKEEI FGPVMQILKF KSMEEVVGRA NNSKYGLAAA
460 470 480 490 500
VFTKDLDKAN YLSQALQAGT VWVNCYDVFG AQSPFGGYKL SGSGRELGEY
510 520
GLQAYTEVKT VTVRVPQKNS
Length:520
Mass (Da):56,653
Last modified:July 1, 2008 - v2
Checksum:i713FC1EE8F82B2C4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti289L → I no nucleotide entry (PubMed:1689984).Curated1
Sequence conflicti289L → I no nucleotide entry (PubMed:2540003).Curated1
Sequence conflicti385A → L no nucleotide entry (PubMed:1689984).Curated1
Sequence conflicti385A → L no nucleotide entry (PubMed:2540003).Curated1
Sequence conflicti409V → L no nucleotide entry (PubMed:1689984).Curated1
Sequence conflicti409V → L no nucleotide entry (PubMed:2540003).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC116084 mRNA. Translation: AAI16085.1.
PIRiS09030.
RefSeqiNP_001068835.1. NM_001075367.1.
UniGeneiBt.44041.

Genome annotation databases

EnsembliENSBTAT00000011521; ENSBTAP00000011521; ENSBTAG00000008743.
GeneIDi508629.
KEGGibta:508629.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC116084 mRNA. Translation: AAI16085.1.
PIRiS09030.
RefSeqiNP_001068835.1. NM_001075367.1.
UniGeneiBt.44041.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A4ZX-ray2.75A/B/C/D22-520[»]
1AG8X-ray2.65A/B/C/D22-520[»]
ProteinModelPortaliP20000.
SMRiP20000.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000011521.

Proteomic databases

PaxDbiP20000.
PeptideAtlasiP20000.
PRIDEiP20000.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000011521; ENSBTAP00000011521; ENSBTAG00000008743.
GeneIDi508629.
KEGGibta:508629.

Organism-specific databases

CTDi217.

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP20000.
KOiK00128.
OMAiTIACGGE.
OrthoDBiEOG091G05E8.
TreeFamiTF300455.

Enzyme and pathway databases

UniPathwayiUPA00780; UER00768.
ReactomeiR-BTA-380612. Metabolism of serotonin.
R-BTA-71384. Ethanol oxidation.
SABIO-RKP20000.

Miscellaneous databases

EvolutionaryTraceiP20000.

Gene expression databases

BgeeiENSBTAG00000008743.

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.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALDH2_BOVIN
AccessioniPrimary (citable) accession number: P20000
Secondary accession number(s): Q1LZC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 1, 2008
Last modified: November 30, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.