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Protein

Alcohol dehydrogenase E chain

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

Functioni

Catalytic activityi

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

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi47Zinc 1; catalyticCombined sources2 Publications1
Metal bindingi49Zinc 1By similarity1
Binding sitei49NADBy similarity1
Binding sitei49SubstrateCombined sources1
Metal bindingi68Zinc 1; catalyticCombined sources2 Publications1
Binding sitei68SubstrateCombined sources1
Metal bindingi98Zinc 2Combined sources2 Publications1
Metal bindingi101Zinc 2Combined sources2 Publications1
Metal bindingi104Zinc 2Combined sources2 Publications1
Metal bindingi112Zinc 2Combined sources2 Publications1
Metal bindingi175Zinc 1; catalyticCombined sources1 Publication1
Binding sitei224NADCombined sources1 Publication1
Binding sitei229NADCombined sources1 Publication1
Binding sitei293NAD; via carbonyl oxygenBy similarity1
Binding sitei320NAD; via amide nitrogenBy similarity1
Binding sitei370NADCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi200 – 205NADCombined sources1 Publication6
Nucleotide bindingi293 – 295NADCombined sources1 Publication3

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BRENDAi1.1.1.1. 2120.
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
Proteomesi
  • UP000002281 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2111372.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001606562 – 375Alcohol dehydrogenase E chainAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP00327.
PeptideAtlasiP00327.
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

1375
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Beta strandi8 – 15Combined sources8
Beta strandi17 – 19Combined sources3
Beta strandi23 – 29Combined sources7
Beta strandi36 – 45Combined sources10
Helixi48 – 54Combined sources7
Beta strandi56 – 58Combined sources3
Beta strandi62 – 64Combined sources3
Beta strandi69 – 77Combined sources9
Beta strandi89 – 92Combined sources4
Beta strandi99 – 101Combined sources3
Helixi102 – 105Combined sources4
Beta strandi106 – 108Combined sources3
Beta strandi116 – 119Combined sources4
Beta strandi125 – 127Combined sources3
Beta strandi130 – 133Combined sources4
Beta strandi136 – 139Combined sources4
Turni142 – 144Combined sources3
Beta strandi147 – 154Combined sources8
Helixi155 – 157Combined sources3
Beta strandi158 – 160Combined sources3
Helixi167 – 170Combined sources4
Helixi171 – 174Combined sources4
Helixi176 – 185Combined sources10
Turni186 – 188Combined sources3
Beta strandi195 – 199Combined sources5
Helixi203 – 214Combined sources12
Beta strandi218 – 223Combined sources6
Helixi227 – 229Combined sources3
Helixi230 – 235Combined sources6
Beta strandi239 – 242Combined sources4
Helixi244 – 246Combined sources3
Helixi251 – 258Combined sources8
Beta strandi263 – 268Combined sources6
Helixi273 – 282Combined sources10
Turni285 – 287Combined sources3
Beta strandi289 – 292Combined sources4
Beta strandi297 – 299Combined sources3
Beta strandi302 – 304Combined sources3
Helixi307 – 310Combined sources4
Beta strandi314 – 317Combined sources4
Helixi320 – 322Combined sources3
Helixi325 – 337Combined sources13
Beta strandi338 – 341Combined sources4
Helixi344 – 346Combined sources3
Beta strandi347 – 352Combined sources6
Helixi353 – 355Combined sources3
Helixi356 – 364Combined sources9
Beta strandi365 – 367Combined sources3
Beta strandi369 – 374Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XD2X-ray1.10A/B2-375[»]
5ADHX-ray2.90A2-375[»]
5CDGX-ray1.40A/B2-375[»]
5CDSX-ray1.40A/B2-375[»]
5CDTX-ray1.70A/B2-375[»]
5CDUX-ray1.60A/B2-375[»]
5KCPX-ray1.10A/B2-375[»]
5KCZX-ray1.14A/B2-375[»]
5KJ1X-ray1.20A/B2-375[»]
5KJ6X-ray1.14A/B2-375[»]
5KJCX-ray1.20A/B2-375[»]
5KJEX-ray1.26A/B2-375[»]
5KJFX-ray1.20A/B2-375[»]
6ADHX-ray2.90A/B2-375[»]
7ADHX-ray3.20A2-375[»]
8ADHX-ray2.40A2-375[»]
ProteinModelPortaliP00327.
SMRiP00327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00327.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
HOGENOMiHOG000294674.
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.

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
PDB 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[»]
4XD2X-ray1.10A/B2-375[»]
5ADHX-ray2.90A2-375[»]
5CDGX-ray1.40A/B2-375[»]
5CDSX-ray1.40A/B2-375[»]
5CDTX-ray1.70A/B2-375[»]
5CDUX-ray1.60A/B2-375[»]
5KCPX-ray1.10A/B2-375[»]
5KCZX-ray1.14A/B2-375[»]
5KJ1X-ray1.20A/B2-375[»]
5KJ6X-ray1.14A/B2-375[»]
5KJCX-ray1.20A/B2-375[»]
5KJEX-ray1.26A/B2-375[»]
5KJFX-ray1.20A/B2-375[»]
6ADHX-ray2.90A/B2-375[»]
7ADHX-ray3.20A2-375[»]
8ADHX-ray2.40A2-375[»]
ProteinModelPortaliP00327.
SMRiP00327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9796.ENSECAP00000017080.

Chemistry databases

ChEMBLiCHEMBL2111372.

Proteomic databases

PaxDbiP00327.
PeptideAtlasiP00327.
PRIDEiP00327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100034242.
KEGGiecb:100034242.

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
KOiK13951.

Enzyme and pathway databases

BRENDAi1.1.1.1. 2120.
SABIO-RKP00327.

Miscellaneous databases

EvolutionaryTraceiP00327.
PROiP00327.

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...

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: November 2, 2016
This is version 142 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

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.