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Protein

Aldehyde dehydrogenase, cytosolic 1

Gene

Aldh1a7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can oxidize benzaldehyde, propionaldehyde and acetaldehyde. No detectable activity with retinal.1 Publication

Catalytic activityi

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

Kineticsi

The highest catalytic efficiency is observed with benzaldehyde as substrate. No activity with retinal.

  1. KM=2.4 mM for acetaldehyde1 Publication
  2. KM=1.6 mM for propionaldehyde1 Publication
  3. KM=4.7 µM for benzaldehyde1 Publication

    Pathway:iethanol 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, cytosolic 1 (Aldh1a7), 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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei170 – 1701Transition state stabilizerBy similarity
    Active sitei269 – 2691Proton acceptorPROSITE-ProRule annotation
    Active sitei303 – 3031NucleophilePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi246 – 2516NADBy similarity

    GO - Molecular functioni

    • 3-chloroallyl aldehyde dehydrogenase activity Source: RGD
    • aldehyde dehydrogenase (NAD) activity Source: RGD
    • benzaldehyde dehydrogenase (NAD+) activity Source: RGD
    • identical protein binding Source: RGD
    • retinal dehydrogenase activity Source: GO_Central

    GO - Biological processi

    • ethanol catabolic process Source: UniProtKB-UniPathway
    • operant conditioning Source: RGD
    • protein homotetramerization Source: RGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    SABIO-RKP13601.
    UniPathwayiUPA00780; UER00768.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldehyde dehydrogenase, cytosolic 1 (EC:1.2.1.3)
    Alternative name(s):
    ALDH class 1
    ALDH-E1
    ALHDII
    Aldehyde dehydrogenase family 1 member A7
    Aldehyde dehydrogenase phenobarbital-inducible
    Gene namesi
    Name:Aldh1a7
    Synonyms:Aldh-pb, Aldh1, Aldh1a4
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494 Componenti: Unplaced

    Organism-specific databases

    RGDi620252. Aldh1a7.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: RGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 501500Aldehyde dehydrogenase, cytosolic 1PRO_0000056426Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei91 – 911N6-acetyllysineBy similarity
    Modified residuei128 – 1281N6-acetyllysineBy similarity
    Modified residuei252 – 2521N6-acetyllysineBy similarity
    Modified residuei353 – 3531N6-acetyllysineBy similarity
    Modified residuei367 – 3671N6-acetyllysineBy similarity
    Modified residuei410 – 4101N6-acetyllysineBy similarity
    Modified residuei413 – 4131PhosphoserineBy similarity
    Modified residuei419 – 4191N6-acetyllysineBy similarity
    Modified residuei435 – 4351N6-acetyllysineBy similarity
    Modified residuei495 – 4951N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiP13601.

    Expressioni

    Tissue specificityi

    Very low levels in lung and liver.1 Publication

    Inductioni

    By phenobarbital.

    Gene expression databases

    GenevisibleiP13601. RN.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP13601.
    SMRiP13601. Positions 9-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Phylogenomic databases

    HOVERGENiHBG000097.
    InParanoidiP13601.
    KOiK07249.
    PhylomeDBiP13601.

    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.

    P13601-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSPAQPAVP APLANLKIQH TKIFINNEWH NSLNGKKFPV INPATEEVIC
    60 70 80 90 100
    HVEEGDKADV DKAVKAARQA FQIGSPWRTM DASERGCLLN KLADLMERDR
    110 120 130 140 150
    VLLATMESMN AGKIFTHAYL LDTEVSIKAL KYFAGWADKI HGQTIPSDGD
    160 170 180 190 200
    VFTYTRREPI GVCGQIIPWN GPLILFIWKI GAALSCGNTV IVKPAEQTPL
    210 220 230 240 250
    TALYMASLIK EAGFPPGVVN VVPGYGSTAG AAISSHMDID KVSFTGSTEV
    260 270 280 290 300
    GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDSAVEF AHQGVFFHQG
    310 320 330 340 350
    QICVAASRLF VEESIYDEFV RRSVERAKKY VLGNPLDSGI SQGPQIDKEQ
    360 370 380 390 400
    HAKILDLIES GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE
    410 420 430 440 450
    IFGPVQQIMK FKSIDEVIKR ANNTPYGLAA GVFTKDLDRA ITVSSALQAG
    460 470 480 490 500
    TVWVNCYLTL SVQCPFGGFK MSGNGREMGE QGVYEYTELK TVAMKISQKN

    S
    Length:501
    Mass (Da):54,560
    Last modified:January 23, 2007 - v2
    Checksum:iE6806A1AF736AF1F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M23995 mRNA. Translation: AAA40718.1.
    PIRiA32616.
    RefSeqiNP_058968.14. NM_017272.15.
    UniGeneiRn.74044.

    Genome annotation databases

    KEGGirno:29651.
    UCSCiRGD:620252. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M23995 mRNA. Translation: AAA40718.1.
    PIRiA32616.
    RefSeqiNP_058968.14. NM_017272.15.
    UniGeneiRn.74044.

    3D structure databases

    ProteinModelPortaliP13601.
    SMRiP13601. Positions 9-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry

    BindingDBiP13601.
    ChEMBLiCHEMBL5354.

    Proteomic databases

    PRIDEiP13601.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGirno:29651.
    UCSCiRGD:620252. rat.

    Organism-specific databases

    RGDi620252. Aldh1a7.

    Phylogenomic databases

    HOVERGENiHBG000097.
    InParanoidiP13601.
    KOiK07249.
    PhylomeDBiP13601.

    Enzyme and pathway databases

    UniPathwayiUPA00780; UER00768.
    SABIO-RKP13601.

    Miscellaneous databases

    PROiP13601.

    Gene expression databases

    GenevisibleiP13601. RN.

    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...

    Publicationsi

    1. "Phenobarbital-inducible aldehyde dehydrogenase in the rat. cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats."
      Dunn T.J., Koleske A.J., Lindahl R., Pitot H.C.
      J. Biol. Chem. 264:13057-13065(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Rat liver constitutive and phenobarbital-inducible cytosolic aldehyde dehydrogenases are highly homologous proteins that function as distinct isozymes."
      Kathmann E.C., Naylor S., Lipsky J.J.
      Biochemistry 39:11170-11176(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiAL1A7_RAT
    AccessioniPrimary (citable) accession number: P13601
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: July 22, 2015
    This is version 111 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

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.