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Protein

Alcohol dehydrogenase S 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; catalytic
Metal bindingi68 – 681Zinc 1; catalytic
Metal bindingi98 – 981Zinc 2
Metal bindingi101 – 1011Zinc 2
Metal bindingi104 – 1041Zinc 2
Metal bindingi112 – 1121Zinc 2
Metal bindingi174 – 1741Zinc 1; catalytic
Binding sitei223 – 2231NAD
Binding sitei228 – 2281NAD
Binding sitei369 – 3691NAD

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi199 – 2046NAD
Nucleotide bindingi292 – 2943NAD

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

SABIO-RKP00328.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase S chain (EC:1.1.1.1)
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2111372.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 374373Alcohol dehydrogenase S chainPRO_0000160657Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP00328.

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
374
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 158Combined sources
Beta strandi23 – 297Combined sources
Beta strandi36 – 4510Combined sources
Helixi48 – 558Combined sources
Beta strandi56 – 583Combined sources
Beta strandi62 – 654Combined sources
Beta strandi69 – 779Combined sources
Beta strandi89 – 924Combined sources
Beta strandi99 – 1013Combined sources
Helixi102 – 1054Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi129 – 1324Combined sources
Beta strandi135 – 1384Combined sources
Turni141 – 1433Combined sources
Beta strandi146 – 1538Combined sources
Helixi154 – 1563Combined sources
Beta strandi157 – 1593Combined sources
Helixi166 – 1694Combined sources
Helixi170 – 1734Combined sources
Helixi175 – 18410Combined sources
Turni185 – 1873Combined sources
Beta strandi194 – 1985Combined sources
Helixi202 – 21312Combined sources
Beta strandi217 – 2226Combined sources
Helixi226 – 2283Combined sources
Helixi229 – 2346Combined sources
Beta strandi238 – 2414Combined sources
Helixi243 – 2453Combined sources
Helixi250 – 2578Combined sources
Beta strandi262 – 2676Combined sources
Helixi272 – 28110Combined sources
Turni284 – 2863Combined sources
Beta strandi288 – 2914Combined sources
Beta strandi301 – 3033Combined sources
Helixi306 – 3094Combined sources
Beta strandi313 – 3164Combined sources
Helixi319 – 3213Combined sources
Helixi324 – 33613Combined sources
Helixi343 – 3453Combined sources
Beta strandi346 – 3516Combined sources
Helixi352 – 3543Combined sources
Helixi355 – 3639Combined sources
Beta strandi368 – 3736Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EE2X-ray1.54A/B2-374[»]
ProteinModelPortaliP00328.
SMRiP00328. Positions 2-374.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00328.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG000195.
KOiK13951.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00328-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTAGKVIKC KAAVLWEQKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD
60 70 80 90 100
DHVVSGTLVA PLPVIAGHEA AGIVESIGEG VTTVRPGDKV IPLFIPQCGK
110 120 130 140 150
CSVCKHPEGN LCLKNLSMPR GTMQDGTSRF TCRGKPIHHF LGTSTFSQYT
160 170 180 190 200
VVDEISVAKI DAASPLEKVC LVGCGFSTGY GSAVKVAKVT QGSTCAVFGL
210 220 230 240 250
GGVGLSVIMG CKAAGAARII GVDINKDKFA KAKEVGATEC VNPQDYKKPI
260 270 280 290 300
QEVLTEMSNG GVDFSFEVIG RLDTMVAALS CCQEAYGVSV IVGVPPDSQN
310 320 330 340 350
LSMNPMLLLS GRTWKGAIFG GFKSKDSVPK LVADFMAKKF ALDPLITHVL
360 370
PFEKINEGFD LLRSGKSIRT ILTF
Length:374
Mass (Da):39,623
Last modified:January 23, 2007 - v3
Checksum:i2B15710A038DA013
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441A → T AA sequence (PubMed:5466062).Curated
Sequence conflicti60 – 601A → T AA sequence (PubMed:5466062).Curated
Sequence conflicti116 – 1161L → SL AA sequence (PubMed:5466062).Curated
Sequence conflicti172 – 1721V → I AA sequence (PubMed:5466062).Curated
Sequence conflicti277 – 2771A → T AA sequence (PubMed:5466062).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64865 mRNA. Translation: AAA30932.1.
PIRiB39872. DEHOAS.
RefSeqiNP_001075414.1. NM_001081945.1.
UniGeneiEca.13101.

Genome annotation databases

GeneIDi100034175.
KEGGiecb:100034175.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64865 mRNA. Translation: AAA30932.1.
PIRiB39872. DEHOAS.
RefSeqiNP_001075414.1. NM_001081945.1.
UniGeneiEca.13101.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EE2X-ray1.54A/B2-374[»]
ProteinModelPortaliP00328.
SMRiP00328. Positions 2-374.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL2111372.

Proteomic databases

PRIDEiP00328.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100034175.
KEGGiecb:100034175.

Phylogenomic databases

HOVERGENiHBG000195.
KOiK13951.

Enzyme and pathway databases

SABIO-RKP00328.

Miscellaneous databases

EvolutionaryTraceiP00328.
PROiP00328.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
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 2-374.
    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).

Entry informationi

Entry nameiADH1S_HORSE
AccessioniPrimary (citable) accession number: P00328
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 128 of the entry and version 3 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

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 one 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.