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Protein

Alcohol dehydrogenase E chain

Gene
N/A
Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 2 Zn2+ 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
Complete GO annotation...

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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
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

        10         20         30         40         50
MSTAGKVIKC KAAVLWEEKK PFSIEEVEVA PPKAHEVRIK MVATGICRSD
60 70 80 90 100
DHVVSGTLVT PLPVIAGHEA AGIVESIGEG VTTVRPGDKV IPLFTPQCGK
110 120 130 140 150
CRVCKHPEGN FCLKNDLSMP RGTMQDGTSR FTCRGKPIHH FLGTSTFSQY
160 170 180 190 200
TVVDEISVAK IDAASPLEKV CLIGCGFSTG YGSAVKVAKV TQGSTCAVFG
210 220 230 240 250
LGGVGLSVIM GCKAAGAARI IGVDINKDKF AKAKEVGATE CVNPQDYKKP
260 270 280 290 300
IQEVLTEMSN GGVDFSFEVI GRLDTMVTAL SCCQEAYGVS VIVGVPPDSQ
310 320 330 340 350
NLSMNPMLLL SGRTWKGAIF GGFKSKDSVP KLVADFMAKK FALDPLITHV
360 370
LPFEKINEGF DLLRSGESIR TILTF
Length:375
Mass (Da):39,936
Last modified:January 23, 2007 - v2
Checksum:iDA701D2F6AB69C9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
M64864 mRNA. Translation: AAA30931.1.
PIRiA39872. DEHOAL.
RefSeqiNP_001075997.1. NM_001082528.1.
UniGeneiEca.13101.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

STRINGi9796.ENSECAP00000017080.

Chemistry

ChEMBLiCHEMBL2111372.

Proteomic databases

PRIDEiP00327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100034242.
KEGGiecb:100034242.

Phylogenomic databases

eggNOGiCOG1062.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
KOiK13951.

Enzyme and pathway databases

SABIO-RKP00327.

Miscellaneous databases

EvolutionaryTraceiP00327.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 130 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

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.