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P07754 (ADH3_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase 3
EC=1.1.1.1
Alternative name(s):
Alcohol dehydrogenase III
Short name=ADH III
Gene names
Name:alcC
Synonyms:adh3
ORF Names:AN2286
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalcohol dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Alcohol dehydrogenase 3
PRO_0000160721

Regions

Nucleotide binding180 – 1867NAD By similarity
Nucleotide binding273 – 2753NAD By similarity

Sites

Metal binding441Zinc 1; catalytic By similarity
Metal binding671Zinc 1; catalytic By similarity
Metal binding1001Zinc 2 By similarity
Metal binding1031Zinc 2 By similarity
Metal binding1061Zinc 2 By similarity
Metal binding1141Zinc 2 By similarity
Metal binding1561Zinc 1; catalytic By similarity
Binding site2041NAD By similarity
Binding site2091NAD By similarity
Binding site3451NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P07754 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: AFDE78FE442E3144

FASTA35237,126
        10         20         30         40         50         60 
MSVPEVQWAQ VVEKAGTPPV YKQVPVPKPG PDEILVKMRY SGVCHTDLHA MKGDWPLPSK 

        70         80         90        100        110        120 
MPLIGGHEGA GVVVAKGELV KDEDFKIGDR AGIKWLNGSC LSCEMCMQAD EPLCPHASLS 

       130        140        150        160        170        180 
GYTVDGTFQQ YTIGKAALAS KIPDNVPLDA AAPILCAGIT VYKGLKESGA RPGQTVAIVG 

       190        200        210        220        230        240 
AGGGLGSLAQ QYAKAMGLRT IAIDSGDEKK AMCEQLGAEV FIDFSKSADV VADVKAATPG 

       250        260        270        280        290        300 
GLGAHAVILL AVAEKPFQQA TEYVRSHGSV VAIGLPANAF LKAPVFTTVV RMINIKGSYV 

       310        320        330        340        350 
GNRQDGVEAL DFFARGLIKA PFKKAPLQDL PQIFELMGQG KIAGRYVLEI PE

« Hide

References

« Hide 'large scale' references
[1]"Identification and molecular analysis of a third Aspergillus nidulans alcohol dehydrogenase gene."
McKnight L., Kato H., Upshall A., Parker M.D., O'Hara P.J., O'Hara S.
EMBO J. 4:2093-2099(1985) [PubMed: 2998782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X02764 Genomic DNA. Translation: CAA26541.1.
AACD01000038 Genomic DNA. Translation: EAA64397.1.
BN001307 Genomic DNA. Translation: CBF86535.1.
PIRA24648.
RefSeqXP_659890.1. XM_654798.1.

3D structure databases

ProteinModelPortalP07754.
SMRP07754. Positions 2-352.
ModBaseSearch...

Protein-protein interaction databases

STRINGP07754.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00008978; CADANIAP00008978; CADANIAG00008978.
GeneID2874791.
KEGGani:AN2286.2.

Phylogenomic databases

OMAHAANGDW.
OrthoDBEOG4Q5CZM.
PhylomeDBP07754.

Family and domain databases

InterProIPR013149. 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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK13953.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADH3_EMENI
AccessionPrimary (citable) accession number: P07754
Secondary accession number(s): C8VN33, Q5BAZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents