[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; DOI=10.1021/bi00164a031; PubMed=1463738 [NCBI, ExPASy, EBI, Israel, Japan] Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., de Rosa M., Rossi M.; "Thermostable NAD(+)-dependent alcohol dehydrogenase from Sulfolobus solfataricus: gene and protein sequence determination and relationship to other alcohol dehydrogenases."; Biochemistry 31:12514-12523(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; Aravalli R.N.; Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; DOI=10.1073/pnas.141222098; PubMed=11427726 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "The complete genome of the crenarchaeon Sulfolobus solfataricus P2."; Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
[4]	X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). DOI=10.1016/S0022-2836(02)00088-8; PubMed=12051852 [NCBI, ExPASy, EBI, Israel, Japan] Esposito L., Sica F., Raia C.A., Giordano A., Rossi M., Mazzarella L., Zagari A.; "Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 A resolution."; J. Mol. Biol. 318:463-477(2002).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
SUBUNIT: Homodimer and homotetramer.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

S51211; AAB24546.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ010590; CAA09258.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE006850; AAK42665.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A44245; A44245.

RefSeq

NP_343875.1; -.

3D structure databases

PDB

1JVB; X-ray; 1.85 A; A=1-347.	[ExPASy / RCSB / EBI]
1NTO; X-ray; 1.94 A; A/B/C/D/E/H=1-347.	[ExPASy / RCSB / EBI]
1NVG; X-ray; 2.50 A; A=1-347.	[ExPASy / RCSB / EBI]
1R37; X-ray; 2.30 A; A/B=1-347.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1JVB; -.
1NTO; -.
1NVG; -.
1R37; -.

ModBase

P39462.

Enzyme and pathway databases

BioCyc

SSOL273057:SSO2536-MON; -.

Ontologies

GO:0004022;	Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00059; ADH_ZINC; 1.

ProtoNet

P39462.

Genome annotation databases

GeneID

1453992; -.

GenomeReviews

AE006641_GR; SSO2536.

KEGG

sso:SSO2536; -.

NMPDR

fig|273057.1.peg.2298; -.

Phylogenomic databases

HOGENOM

P39462; -.

Genome annotation databases

CMR

P39462; SSO2536.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Direct protein sequencing; Metal-binding; Methylation; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 347`	`347`	`NAD-dependent alcohol dehydrogenase.`	`PRO_0000160753`
`METAL`	`38 38`		`Zinc 1; catalytic.`
`METAL`	`68 68`		`Zinc 1; catalytic.`
`METAL`	`98 98`		`Zinc 2.`
`METAL`	`101 101`		`Zinc 2.`
`METAL`	`104 104`		`Zinc 2.`
`METAL`	`112 112`		`Zinc 2.`
`METAL`	`154 154`		`Zinc 1; catalytic.`
`MOD_RES`	`11 11`		`N6-methyllysine; partial.`
`MOD_RES`	`213 213`		`N6-methyllysine; partial.`
`STRAND`	`2 6`	`5`
`STRAND`	`14 17`	`4`
`STRAND`	`28 37`	`10`
`HELIX`	`40 44`	`5`
`TURN`	`45 47`	`3`
`TURN`	`54 58`	`5`
`STRAND`	`69 77`	`9`
`STRAND`	`89 92`	`4`
`STRAND`	`99 101`	`3`
`HELIX`	`102 105`	`4`
`HELIX`	`109 111`	`3`
`TURN`	`118 120`	`3`
`STRAND`	`125 133`	`9`
`HELIX`	`135 137`	`3`
`STRAND`	`138 140`	`3`
`STRAND`	`142 144`	`3`
`HELIX`	`146 149`	`4`
`HELIX`	`150 153`	`4`
`HELIX`	`155 165`	`11`
`STRAND`	`173 177`	`5`
`TURN`	`178 180`	`3`
`HELIX`	`182 194`	`13`
`STRAND`	`198 205`	`8`
`HELIX`	`206 215`	`10`
`STRAND`	`218 222`	`5`
`TURN`	`223 225`	`3`
`HELIX`	`228 235`	`8`
`TURN`	`236 238`	`3`
`STRAND`	`241 247`	`7`
`HELIX`	`251 254`	`4`
`HELIX`	`257 260`	`4`
`STRAND`	`261 269`	`9`
`STRAND`	`276 280`	`5`
`HELIX`	`281 287`	`7`
`STRAND`	`290 293`	`4`
`HELIX`	`299 310`	`12`
`STRAND`	`319 323`	`5`
`HELIX`	`324 326`	`3`
`HELIX`	`327 335`	`9`
`STRAND`	`341 346`	`6`

Sequence information

Length: 347 AA [This is the length of the unprocessed precursor]

Molecular weight: 37569 Da [This is the MW of the unprocessed precursor]

CRC64: 755848A249D4F4A2 [This is a checksum on the sequence]

        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

P39462 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools