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Reviewed, UniProtKB/Swiss-Prot P39462 (ADH_SULSO)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    NAD-dependent alcohol dehydrogenase
    EC=1.1.1.1
Gene names
Name: adh
Ordered Locus Names: SSO2536
OrganismSulfolobus solfataricus [Complete proteome] [HAMAP]
Taxonomic identifier2287 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

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Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer and homotetramer.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

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Ontologies

Keywords
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   PTMMethylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalcohol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347NAD-dependent alcohol dehydrogenase
PRO_0000160753

Sites

Metal binding381Zinc 1; catalytic
Metal binding681Zinc 1; catalytic
Metal binding981Zinc 2
Metal binding1011Zinc 2
Metal binding1041Zinc 2
Metal binding1121Zinc 2
Metal binding1541Zinc 1; catalytic

Amino acid modifications

Modified residue111N6-methyllysine; partial
Modified residue2131N6-methyllysine; partial

Secondary structure

1 ..................................................................... 347
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P39462-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 755848A249D4F4A2

FASTA34737,569
        10         20         30         40         50         60 
MRAVRLVEIG KPLSLQEIGV PKPKGPQVLI KVEAAGVCHS DVHMRQGRFG NLRIVEDLGV 

        70         80         90        100        110        120 
KLPVTLGHEI AGKIEEVGDE VVGYSKGDLV AVNPWQGEGN CYYCRIGEEH LCDSPRWLGI 

       130        140        150        160        170        180 
NFDGAYAEYV IVPHYKYMYK LRRLNAVEAA PLTCSGITTY RAVRKASLDP TKTLLVVGAG 

       190        200        210        220        230        240 
GGLGTMAVQI AKAVSGATII GVDVREEAVE AAKRAGADYV INASMQDPLA EIRRITESKG 

       250        260        270        280        290        300 
VDAVIDLNNS EKTLSVYPKA LAKQGKYVMV GLFGADLHYH APLITLSEIQ FVGSLVGNQS 

       310        320        330        340 
DFLGIMRLAE AGKVKPMITK TMKLEEANEA IDNLENFKAI GRQVLIP

« Hide

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References

« Hide 'large scale' references
[1]"Thermostable NAD(+)-dependent alcohol dehydrogenase from Sulfolobus solfataricus: gene and protein sequence determination and relationship to other alcohol dehydrogenases."
Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., de Rosa M., Rossi M.
Biochemistry 31:12514-12523(1992) [PubMed: 1463738] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[2]Aravalli R.N.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[3]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed: 11427726] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[4]"Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 A resolution."
Esposito L., Sica F., Raia C.A., Giordano A., Rossi M., Mazzarella L., Zagari A.
J. Mol. Biol. 318:463-477(2002) [PubMed: 12051852] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

S51211 Genomic DNA. Translation: AAB24546.1.
AJ010590 Genomic DNA. Translation: CAA09258.1.
AE006641 Genomic DNA. Translation: AAK42665.1.
PIRA44245.
RefSeqNP_343875.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JVBX-ray1.85A1-347[»]
1NTOX-ray1.94A/B/C/D/E/H1-347[»]
1NVGX-ray2.50A1-347[»]
1R37X-ray2.30A/B1-347[»]
ModBaseSearch...

Genome annotation databases

GeneID1453992.
GenomeReviewsGene locus SSO2536 in contig AE006641_GR.
KEGGsso:SSO2536.
NMPDRfig|273057.1.peg.2298.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP39462.
OMAP39462. DYVINAS.

Enzyme and pathway databases

BioCycSSOL273057:SSO2536-MON.
BRENDA1.1.1.1. 2070.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameADH_SULSO
AccessionPrimary (citable) accession number: P39462
Secondary accession number(s): O74076
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents