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P20000

- ALDH2_BOVIN

UniProt

P20000 - ALDH2_BOVIN

Protein

Aldehyde dehydrogenase, mitochondrial

Gene

ALDH2

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (01 Jul 2008)
      Previous versions | rss
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    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

    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. mitochondrial matrix Source: UniProtKB-SubCell

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00550000074289.
    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

    MLRAVALAAA RLGPRQGRRL LSAATQAVPT PNQQPEVLYN QIFINNEWHD    50
    AVSKKTFPTV NPSTGDVICH VAEGDKADVD RAVKAARAAF QLGSPWRRMD 100
    ASERGRLLNR LADLIERDRT YLAALETLDN GKPYIISYLV DLDMVLKCLR 150
    YYAGWADKYH GKTIPIDGDY FSYTRHEPVG VCGQIIPWNF PLLMQAWKLG 200
    PALATGNVVV MKVAEQTPLT ALYVANLIKE AGFPPGVVNV IPGFGPTAGA 250
    AIASHEDVDK VAFTGSTEVG HLIQVAAGKS NLKRVTLELG GKSPNIIMSD 300
    ADMDWAVEQA HFALFFNQGQ CCCAGSRTFV QEDIYAEFVE RSVARAKSRV 350
    VGNPFDSRTE QGPQVDETQF KKVLGYIKSG KEEGAKLLCG GGAAADRGYF 400
    IQPTVFGDVQ DGMTIAKEEI FGPVMQILKF KSMEEVVGRA NNSKYGLAAA 450
    VFTKDLDKAN YLSQALQAGT VWVNCYDVFG AQSPFGGYKL SGSGRELGEY 500
    GLQAYTEVKT VTVRVPQKNS 520
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 ENSGT00550000074289.
    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

    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: October 1, 2014
    This is version 115 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