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P39462 (ADH_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

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...

Sequences

Sequence LengthMass (Da)Tools
P39462 [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

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S51211 Genomic DNA. Translation: AAB24546.1.
AJ010590 Genomic DNA. Translation: CAA09258.1.
AE006641 Genomic DNA. Translation: AAK42665.1.
PIRA44245.
RefSeqNP_343875.1. NC_002754.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
3I4CX-ray2.00A/B/C/D/E/H1-347[»]
ProteinModelPortalP39462.
SMRP39462. Positions 1-347.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMHBG753318.
OMAISERATP.
ProtClustDBCLSK883800.

Enzyme and pathway databases

BioCycSSOL273057:SSO2536-MONOMER.

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.
KOK00001.
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 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: December 14, 2011
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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