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P00327

- ADH1E_HORSE

UniProt

P00327 - ADH1E_HORSE

Protein

Alcohol dehydrogenase E chain

Gene
N/A
Organism
Equus caballus (Horse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    An alcohol + NAD+ = an aldehyde or ketone + NADH.

    Cofactori

    Binds 2 zinc ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi47 – 471Zinc 1; catalytic1 Publication
    Metal bindingi68 – 681Zinc 1; catalytic1 Publication
    Metal bindingi98 – 981Zinc 21 Publication
    Metal bindingi101 – 1011Zinc 21 Publication
    Metal bindingi104 – 1041Zinc 21 Publication
    Metal bindingi112 – 1121Zinc 21 Publication
    Metal bindingi175 – 1751Zinc 1; catalytic
    Binding sitei224 – 2241NAD
    Binding sitei229 – 2291NAD
    Binding sitei370 – 3701NAD

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi200 – 2056NAD
    Nucleotide bindingi293 – 2953NAD

    GO - Molecular functioni

    1. alcohol dehydrogenase (NAD) activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    SABIO-RKP00327.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase E chain (EC:1.1.1.1)
    OrganismiEquus caballus (Horse)
    Taxonomic identifieri9796 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
    ProteomesiUP000002281: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 375374Alcohol dehydrogenase E chainPRO_0000160656Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP00327.

    Interactioni

    Subunit structurei

    Dimer of identical or non-identical chains of two types (E and S) coded by 2 separate genes at different loci.

    Protein-protein interaction databases

    STRINGi9796.ENSECAP00000017080.

    Structurei

    Secondary structure

    1
    375
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53
    Beta strandi8 – 158
    Beta strandi17 – 193
    Beta strandi23 – 297
    Beta strandi36 – 4510
    Helixi48 – 547
    Beta strandi56 – 583
    Beta strandi62 – 643
    Beta strandi69 – 779
    Beta strandi89 – 924
    Beta strandi99 – 1013
    Helixi102 – 1054
    Beta strandi106 – 1083
    Beta strandi116 – 1194
    Beta strandi125 – 1273
    Beta strandi130 – 1334
    Beta strandi136 – 1394
    Turni142 – 1443
    Beta strandi147 – 1548
    Helixi155 – 1573
    Beta strandi158 – 1603
    Helixi167 – 1704
    Helixi171 – 1744
    Helixi176 – 18510
    Turni186 – 1883
    Beta strandi195 – 1995
    Helixi203 – 21412
    Beta strandi218 – 2236
    Helixi227 – 2293
    Helixi230 – 2356
    Beta strandi239 – 2424
    Helixi244 – 2463
    Helixi251 – 2588
    Beta strandi263 – 2686
    Helixi273 – 28210
    Turni285 – 2873
    Beta strandi289 – 2924
    Beta strandi297 – 2993
    Beta strandi302 – 3043
    Helixi307 – 3104
    Beta strandi314 – 3174
    Helixi320 – 3223
    Helixi325 – 33713
    Beta strandi338 – 3414
    Helixi344 – 3463
    Beta strandi347 – 3526
    Helixi353 – 3553
    Helixi356 – 3649
    Beta strandi365 – 3673
    Beta strandi369 – 3746

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A71X-ray2.00A/B2-375[»]
    1A72X-ray2.60A2-375[»]
    1ADBX-ray2.40A/B2-375[»]
    1ADCX-ray2.70A/B2-375[»]
    1ADFX-ray2.90A2-375[»]
    1ADGX-ray2.70A2-375[»]
    1AXEX-ray2.00A/B2-375[»]
    1AXGX-ray2.50A/B/C/D2-375[»]
    1BTOX-ray2.00A/B/C/D2-375[»]
    1HETX-ray1.15A/B2-375[»]
    1HEUX-ray1.15A/B2-375[»]
    1HF3X-ray1.95A/B2-375[»]
    1HLDX-ray2.10A/B2-375[»]
    1JU9X-ray2.00A/B2-375[»]
    1LDEX-ray2.50A/B/C/D2-375[»]
    1LDYX-ray2.50A/B/C/D2-375[»]
    1MG0X-ray1.80A/B/C/D2-375[»]
    1MGOX-ray1.20A/B2-375[»]
    1N8KX-ray1.13A/B2-375[»]
    1N92X-ray1.47A/B2-375[»]
    1P1RX-ray1.57A/B/C/D2-375[»]
    1QLHX-ray2.07A2-375[»]
    1QLJX-ray2.80A2-375[»]
    1QV6X-ray1.80A/B2-375[»]
    1QV7X-ray1.80A/B2-375[»]
    1YE3X-ray1.59A2-375[»]
    2JHFX-ray1.00A/B2-375[»]
    2JHGX-ray1.20A/B2-375[»]
    2OHXX-ray1.80A/B2-375[»]
    2OXIX-ray2.10A/B2-375[»]
    3BTOX-ray1.66A/B/C/D2-375[»]
    3OQ6X-ray1.20A/B2-375[»]
    4DWVX-ray1.14A/B2-375[»]
    4DXHX-ray1.12A/B2-375[»]
    4NFHX-ray1.20A/B2-375[»]
    4NFSX-ray1.10A/B2-375[»]
    4NG5X-ray1.10A/B2-375[»]
    5ADHX-ray2.90A2-375[»]
    6ADHX-ray2.90A/B2-375[»]
    7ADHX-ray3.20A2-375[»]
    8ADHX-ray2.40A2-375[»]
    ProteinModelPortaliP00327.
    SMRiP00327. Positions 2-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00327.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1062.
    HOGENOMiHOG000294674.
    HOVERGENiHBG000195.
    InParanoidiP00327.
    KOiK13951.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_GroES-like.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 2 hits.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00327-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTAGKVIKC KAAVLWEEKK PFSIEEVEVA PPKAHEVRIK MVATGICRSD    50
    DHVVSGTLVT PLPVIAGHEA AGIVESIGEG VTTVRPGDKV IPLFTPQCGK 100
    CRVCKHPEGN FCLKNDLSMP RGTMQDGTSR FTCRGKPIHH FLGTSTFSQY 150
    TVVDEISVAK IDAASPLEKV CLIGCGFSTG YGSAVKVAKV TQGSTCAVFG 200
    LGGVGLSVIM GCKAAGAARI IGVDINKDKF AKAKEVGATE CVNPQDYKKP 250
    IQEVLTEMSN GGVDFSFEVI GRLDTMVTAL SCCQEAYGVS VIVGVPPDSQ 300
    NLSMNPMLLL SGRTWKGAIF GGFKSKDSVP KLVADFMAKK FALDPLITHV 350
    LPFEKINEGF DLLRSGESIR TILTF 375
    Length:375
    Mass (Da):39,936
    Last modified:January 23, 2007 - v2
    Checksum:iDA701D2F6AB69C9D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64864 mRNA. Translation: AAA30931.1.
    PIRiA39872. DEHOAL.
    RefSeqiNP_001075997.1. NM_001082528.1.
    UniGeneiEca.13101.

    Genome annotation databases

    GeneIDi100034242.
    KEGGiecb:100034242.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64864 mRNA. Translation: AAA30931.1 .
    PIRi A39872. DEHOAL.
    RefSeqi NP_001075997.1. NM_001082528.1.
    UniGenei Eca.13101.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A71 X-ray 2.00 A/B 2-375 [» ]
    1A72 X-ray 2.60 A 2-375 [» ]
    1ADB X-ray 2.40 A/B 2-375 [» ]
    1ADC X-ray 2.70 A/B 2-375 [» ]
    1ADF X-ray 2.90 A 2-375 [» ]
    1ADG X-ray 2.70 A 2-375 [» ]
    1AXE X-ray 2.00 A/B 2-375 [» ]
    1AXG X-ray 2.50 A/B/C/D 2-375 [» ]
    1BTO X-ray 2.00 A/B/C/D 2-375 [» ]
    1HET X-ray 1.15 A/B 2-375 [» ]
    1HEU X-ray 1.15 A/B 2-375 [» ]
    1HF3 X-ray 1.95 A/B 2-375 [» ]
    1HLD X-ray 2.10 A/B 2-375 [» ]
    1JU9 X-ray 2.00 A/B 2-375 [» ]
    1LDE X-ray 2.50 A/B/C/D 2-375 [» ]
    1LDY X-ray 2.50 A/B/C/D 2-375 [» ]
    1MG0 X-ray 1.80 A/B/C/D 2-375 [» ]
    1MGO X-ray 1.20 A/B 2-375 [» ]
    1N8K X-ray 1.13 A/B 2-375 [» ]
    1N92 X-ray 1.47 A/B 2-375 [» ]
    1P1R X-ray 1.57 A/B/C/D 2-375 [» ]
    1QLH X-ray 2.07 A 2-375 [» ]
    1QLJ X-ray 2.80 A 2-375 [» ]
    1QV6 X-ray 1.80 A/B 2-375 [» ]
    1QV7 X-ray 1.80 A/B 2-375 [» ]
    1YE3 X-ray 1.59 A 2-375 [» ]
    2JHF X-ray 1.00 A/B 2-375 [» ]
    2JHG X-ray 1.20 A/B 2-375 [» ]
    2OHX X-ray 1.80 A/B 2-375 [» ]
    2OXI X-ray 2.10 A/B 2-375 [» ]
    3BTO X-ray 1.66 A/B/C/D 2-375 [» ]
    3OQ6 X-ray 1.20 A/B 2-375 [» ]
    4DWV X-ray 1.14 A/B 2-375 [» ]
    4DXH X-ray 1.12 A/B 2-375 [» ]
    4NFH X-ray 1.20 A/B 2-375 [» ]
    4NFS X-ray 1.10 A/B 2-375 [» ]
    4NG5 X-ray 1.10 A/B 2-375 [» ]
    5ADH X-ray 2.90 A 2-375 [» ]
    6ADH X-ray 2.90 A/B 2-375 [» ]
    7ADH X-ray 3.20 A 2-375 [» ]
    8ADH X-ray 2.40 A 2-375 [» ]
    ProteinModelPortali P00327.
    SMRi P00327. Positions 2-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9796.ENSECAP00000017080.

    Chemistry

    BindingDBi P00327.
    ChEMBLi CHEMBL2111372.

    Proteomic databases

    PRIDEi P00327.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100034242.
    KEGGi ecb:100034242.

    Phylogenomic databases

    eggNOGi COG1062.
    HOGENOMi HOG000294674.
    HOVERGENi HBG000195.
    InParanoidi P00327.
    KOi K13951.

    Enzyme and pathway databases

    SABIO-RK P00327.

    Miscellaneous databases

    EvolutionaryTracei P00327.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProi IPR013149. ADH_C.
    IPR013154. ADH_GroES-like.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11695. PTHR11695. 1 hit.
    Pfami PF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50129. SSF50129. 2 hits.
    PROSITEi PS00059. ADH_ZINC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and steroids. cDNA cloning, expression, and comparison of active sites."
      Park D.H., Plapp B.V.
      J. Biol. Chem. 266:13296-13302(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Horse liver alcohol dehydrogenase. On the primary structures of the isoenzymes."
      Joernvall H.
      Eur. J. Biochem. 16:41-49(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-375.
      Tissue: Liver.
    3. "Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4-A resolution."
      Eklund H., Nordstroem B., Zeppezauer E., Soederlund G., Ohlsson I., Boiwe T., Soederberg B.-O., Tapia O., Braenden C.-I., Aakeson A.
      J. Mol. Biol. 102:27-59(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    4. "Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase."
      Eklund H., Samama J.-P., Jones T.A.
      Biochemistry 23:5982-5996(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
    5. "Refined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8-A resolution."
      Al-Karadaghi S., Cedergren-Zeppezauer E.S., Hovmoeller S., Petratos K., Terry H., Wilson K.S.
      Acta Crystallogr. D 50:793-807(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiADH1E_HORSE
    AccessioniPrimary (citable) accession number: P00327
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3