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P20000

- ALDH2_BOVIN

UniProt

P20000 - ALDH2_BOVIN

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Protein

Aldehyde dehydrogenase, mitochondrial

Gene

ALDH2

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

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei189 – 1891Transition state stabilizer
Active sitei288 – 2881Proton acceptor
Active sitei322 – 3221Nucleophile

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi265 – 2706NADBy similarity

GO - Molecular functioni

  1. aldehyde dehydrogenase (NAD) activity Source: UniProtKB-EC

GO - Biological processi

  1. ethanol catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_215931. Ethanol oxidation.
REACT_227135. Metabolism of serotonin.
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
ProteomesiUP000009136: Chromosome 17

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2121Mitochondrion1 PublicationAdd
BLAST
Chaini22 – 520499Aldehyde dehydrogenase, mitochondrialPRO_0000007167Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-acetyllysineBy similarity
Modified residuei76 – 761N6-acetyllysineBy similarity
Modified residuei162 – 1621N6-acetyllysineBy similarity
Modified residuei371 – 3711N6-acetyllysineBy similarity
Modified residuei378 – 3781N6-acetyllysineBy similarity
Modified residuei386 – 3861N6-acetyllysineBy similarity
Modified residuei429 – 4291N6-acetyllysineBy similarity
Modified residuei431 – 4311N6-acetyllysineBy similarity
Modified residuei444 – 4441N6-acetyllysineBy similarity
Modified residuei454 – 4541N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP20000.
PRIDEiP20000.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000011521.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 466Combined sources
Beta strandi47 – 493Combined sources
Beta strandi56 – 605Combined sources
Turni62 – 643Combined sources
Beta strandi67 – 726Combined sources
Helixi76 – 8914Combined sources
Helixi95 – 984Combined sources
Helixi101 – 11717Combined sources
Helixi119 – 13012Combined sources
Helixi134 – 1396Combined sources
Helixi141 – 15313Combined sources
Turni154 – 1585Combined sources
Beta strandi161 – 1644Combined sources
Beta strandi167 – 17812Combined sources
Beta strandi181 – 1855Combined sources
Beta strandi188 – 1903Combined sources
Helixi191 – 20515Combined sources
Beta strandi208 – 2136Combined sources
Helixi219 – 23113Combined sources
Beta strandi237 – 2437Combined sources
Helixi245 – 2539Combined sources
Beta strandi260 – 2656Combined sources
Helixi267 – 27913Combined sources
Beta strandi284 – 2885Combined sources
Beta strandi294 – 2974Combined sources
Helixi303 – 31513Combined sources
Helixi316 – 3194Combined sources
Beta strandi327 – 3315Combined sources
Helixi332 – 34817Combined sources
Helixi367 – 38317Combined sources
Beta strandi386 – 3894Combined sources
Beta strandi392 – 3943Combined sources
Beta strandi396 – 3983Combined sources
Beta strandi404 – 4085Combined sources
Helixi414 – 4174Combined sources
Beta strandi422 – 4309Combined sources
Helixi433 – 4419Combined sources
Beta strandi447 – 4526Combined sources
Helixi456 – 46510Combined sources
Beta strandi469 – 4746Combined sources
Beta strandi492 – 4943Combined sources
Helixi500 – 5034Combined sources
Beta strandi506 – 5149Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4ZX-ray2.75A/B/C/D22-520[»]
1AG8X-ray2.65A/B/C/D22-520[»]
ProteinModelPortaliP20000.
SMRiP20000. Positions 28-520.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20000.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP20000.
KOiK00128.
OMAiYINTGKQ.
OrthoDBiEOG7PS1F7.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti289 – 2891L → I no nucleotide entry (PubMed:1689984)Curated
Sequence conflicti289 – 2891L → I no nucleotide entry (PubMed:2540003)Curated
Sequence conflicti385 – 3851A → L no nucleotide entry (PubMed:1689984)Curated
Sequence conflicti385 – 3851A → L no nucleotide entry (PubMed:2540003)Curated
Sequence conflicti409 – 4091V → L no nucleotide entry (PubMed:1689984)Curated
Sequence conflicti409 – 4091V → L no nucleotide entry (PubMed:2540003)Curated

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 .
PIRi S09030.
RefSeqi NP_001068835.1. NM_001075367.1.
UniGenei Bt.44041.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A4Z X-ray 2.75 A/B/C/D 22-520 [» ]
1AG8 X-ray 2.65 A/B/C/D 22-520 [» ]
ProteinModelPortali P20000.
SMRi P20000. Positions 28-520.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000011521.

Proteomic databases

PaxDbi P20000.
PRIDEi P20000.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000011521 ; ENSBTAP00000011521 ; ENSBTAG00000008743 .
GeneIDi 508629.
KEGGi bta:508629.

Organism-specific databases

CTDi 217.

Phylogenomic databases

eggNOGi COG1012.
GeneTreei ENSGT00760000118999.
HOGENOMi HOG000271505.
HOVERGENi HBG000097.
InParanoidi P20000.
KOi K00128.
OMAi YINTGKQ.
OrthoDBi EOG7PS1F7.
TreeFami TF300455.

Enzyme and pathway databases

UniPathwayi UPA00780 ; UER00768 .
Reactomei REACT_215931. Ethanol oxidation.
REACT_227135. Metabolism of serotonin.
SABIO-RK P20000.

Miscellaneous databases

EvolutionaryTracei P20000.
NextBioi 20868609.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProi IPR016161. 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 ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the precursor of bovine liver mitochondrial aldehyde dehydrogenase as determined from its cDNA, its gene, and its functionality."
    Guan K., Weiner H.
    Arch. Biochem. Biophys. 277:351-360(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Ascending colon.
  3. "Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences."
    Farres J., Guan K.-L., Weiner H.
    Eur. J. Biochem. 180:67-74(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 92-520.
  4. "Purification and characterization of bovine brain gamma-aminobutyraldehyde dehydrogenase."
    Lee J.E., Cho Y.D.
    Biochem. Biophys. Res. Commun. 189:450-454(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-34.
    Tissue: Brain.
  5. "Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion."
    Steinmetz C.G., Xie P., Weiner H., Hurley T.D.
    Structure 5:701-711(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).

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 26, 2014
This is version 117 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

External Data

Dasty 3