Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NADP-dependent alcohol dehydrogenase 6

Gene

ADH6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

NADP-dependent alcohol dehydrogenase with a broad substrate specificity.

Catalytic activityi

An alcohol + NADP+ = an aldehyde + NADPH.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi46 – 461Zinc 1; catalyticBy similarity
Metal bindingi68 – 681Zinc 1; catalyticBy similarity
Metal bindingi100 – 1001Zinc 2By similarity
Metal bindingi103 – 1031Zinc 2By similarity
Metal bindingi106 – 1061Zinc 2By similarity
Metal bindingi114 – 1141Zinc 2By similarity
Metal bindingi163 – 1631Zinc 1; catalyticBy similarity
Binding sitei215 – 2151NADBy similarity
Binding sitei348 – 3481NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi187 – 1926NADBy similarity
Nucleotide bindingi275 – 2773NADBy similarity

GO - Molecular functioni

  • alcohol dehydrogenase (NADP+) activity Source: SGD
  • hydroxymethylfurfural reductase (NADH) activity Source: SGD
  • hydroxymethylfurfural reductase (NADPH) activity Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • alcohol metabolic process Source: SGD
  • cellular aldehyde metabolic process Source: SGD
  • furaldehyde metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NADP, Zinc

Enzyme and pathway databases

BioCyciYEAST:YMR318C-MONOMER.
SABIO-RKQ04894.

Names & Taxonomyi

Protein namesi
Recommended name:
NADP-dependent alcohol dehydrogenase 6 (EC:1.1.1.2)
Alternative name(s):
NADP-dependent alcohol dehydrogenase VI
ScADHVI
Gene namesi
Name:ADH6
Ordered Locus Names:YMR318C
ORF Names:YM9924.10C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIII

Organism-specific databases

CYGDiYMR318c.
EuPathDBiFungiDB:YMR318C.
SGDiS000004937. ADH6.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360NADP-dependent alcohol dehydrogenase 6PRO_0000160734Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311Phosphoserine1 Publication
Modified residuei315 – 3151PhosphoserineBy similarity
Modified residuei359 – 3591Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04894.
PaxDbiQ04894.
PeptideAtlasiQ04894.

Expressioni

Gene expression databases

GenevestigatoriQ04894.

Interactioni

Protein-protein interaction databases

BioGridi35498. 38 interactions.
DIPiDIP-6308N.
IntActiQ04894. 1 interaction.
MINTiMINT-696048.
STRINGi4932.YMR318C.

Structurei

Secondary structure

1
360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53Combined sources
Beta strandi7 – 126Combined sources
Beta strandi15 – 173Combined sources
Beta strandi22 – 265Combined sources
Beta strandi35 – 4511Combined sources
Helixi47 – 537Combined sources
Turni54 – 574Combined sources
Beta strandi62 – 643Combined sources
Beta strandi70 – 778Combined sources
Beta strandi90 – 934Combined sources
Beta strandi95 – 984Combined sources
Beta strandi101 – 1033Combined sources
Helixi104 – 1074Combined sources
Helixi111 – 1133Combined sources
Beta strandi118 – 1225Combined sources
Beta strandi134 – 1429Combined sources
Helixi143 – 1453Combined sources
Beta strandi146 – 1483Combined sources
Helixi155 – 1584Combined sources
Helixi159 – 1624Combined sources
Helixi164 – 17411Combined sources
Beta strandi182 – 1865Combined sources
Helixi190 – 20213Combined sources
Beta strandi205 – 2139Combined sources
Helixi216 – 2216Combined sources
Beta strandi225 – 2295Combined sources
Helixi230 – 2323Combined sources
Helixi236 – 2394Combined sources
Beta strandi244 – 2496Combined sources
Beta strandi254 – 2563Combined sources
Turni259 – 2613Combined sources
Helixi262 – 2654Combined sources
Beta strandi266 – 2749Combined sources
Beta strandi284 – 2863Combined sources
Helixi288 – 2903Combined sources
Beta strandi295 – 2984Combined sources
Helixi304 – 31613Combined sources
Beta strandi323 – 3297Combined sources
Helixi330 – 34213Combined sources
Beta strandi346 – 3527Combined sources
Helixi355 – 3584Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PIWX-ray3.00A/B1-360[»]
1PS0X-ray3.01A1-360[»]
1Q1NX-ray3.15A1-360[»]
ProteinModelPortaliQ04894.
SMRiQ04894. Positions 1-360.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04894.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1064.
GeneTreeiENSGT00780000122413.
HOGENOMiHOG000294667.
InParanoidiQ04894.
KOiK00002.
OMAiHDIDIKI.
OrthoDBiEOG757D7B.

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. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYPEKFEGI AIQSHEDWKN PKKTKYDPKP FYDHDIDIKI EACGVCGSDI
60 70 80 90 100
HCAAGHWGNM KMPLVVGHEI VGKVVKLGPK SNSGLKVGQR VGVGAQVFSC
110 120 130 140 150
LECDRCKNDN EPYCTKFVTT YSQPYEDGYV SQGGYANYVR VHEHFVVPIP
160 170 180 190 200
ENIPSHLAAP LLCGGLTVYS PLVRNGCGPG KKVGIVGLGG IGSMGTLISK
210 220 230 240 250
AMGAETYVIS RSSRKREDAM KMGADHYIAT LEEGDWGEKY FDTFDLIVVC
260 270 280 290 300
ASSLTDIDFN IMPKAMKVGG RIVSISIPEQ HEMLSLKPYG LKAVSISYSA
310 320 330 340 350
LGSIKELNQL LKLVSEKDIK IWVETLPVGE AGVHEAFERM EKGDVRYRFT
360
LVGYDKEFSD
Length:360
Mass (Da):39,618
Last modified:November 1, 1997 - v1
Checksum:i3F785BE0C5ED8CF1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54141 Genomic DNA. Translation: CAA90836.1.
BK006946 Genomic DNA. Translation: DAA10220.1.
PIRiS59311.
RefSeqiNP_014051.3. NM_001182831.3.

Genome annotation databases

EnsemblFungiiYMR318C; YMR318C; YMR318C.
GeneIDi855368.
KEGGisce:YMR318C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54141 Genomic DNA. Translation: CAA90836.1.
BK006946 Genomic DNA. Translation: DAA10220.1.
PIRiS59311.
RefSeqiNP_014051.3. NM_001182831.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PIWX-ray3.00A/B1-360[»]
1PS0X-ray3.01A1-360[»]
1Q1NX-ray3.15A1-360[»]
ProteinModelPortaliQ04894.
SMRiQ04894. Positions 1-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35498. 38 interactions.
DIPiDIP-6308N.
IntActiQ04894. 1 interaction.
MINTiMINT-696048.
STRINGi4932.YMR318C.

Proteomic databases

MaxQBiQ04894.
PaxDbiQ04894.
PeptideAtlasiQ04894.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR318C; YMR318C; YMR318C.
GeneIDi855368.
KEGGisce:YMR318C.

Organism-specific databases

CYGDiYMR318c.
EuPathDBiFungiDB:YMR318C.
SGDiS000004937. ADH6.

Phylogenomic databases

eggNOGiCOG1064.
GeneTreeiENSGT00780000122413.
HOGENOMiHOG000294667.
InParanoidiQ04894.
KOiK00002.
OMAiHDIDIKI.
OrthoDBiEOG757D7B.

Enzyme and pathway databases

BioCyciYEAST:YMR318C-MONOMER.
SABIO-RKQ04894.

Miscellaneous databases

EvolutionaryTraceiQ04894.
NextBioi979148.
PROiQ04894.

Gene expression databases

GenevestigatoriQ04894.

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. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Crystallization and preliminary X-ray analysis of NADP(H)-dependent alcohol dehydrogenases from Saccharomyces cerevisiae and Rana perezi."
    Valencia E., Rosell A., Larroy C., Farres J., Biosca J.A., Fita I., Pares X., Ochoa W.F.
    Acta Crystallogr. D 59:334-337(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiADH6_YEAST
AccessioniPrimary (citable) accession number: Q04894
Secondary accession number(s): D6W0E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 29, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 21700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

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.