[1]	PROTEIN SEQUENCE. STRAIN=ATCC 53556 / HTD4 / DSM 1457; DOI=10.1021/bi00442a004; PubMed=2790012 [NCBI, ExPASy, EBI, Israel, Japan] Peretz M., Burstein Y.; "Amino acid sequence of alcohol dehydrogenase from the thermophilic bacterium Thermoanaerobium brockii."; Biochemistry 28:6549-6555(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 53556 / HTD4 / DSM 1457; Burstein Y.; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). DOI=10.1006/jmbi.1998.1750; PubMed=9836873 [NCBI, ExPASy, EBI, Israel, Japan] Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F.; "NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii."; J. Mol. Biol. 278:967-981(1998).

Comments

CATALYTIC ACTIVITY: An alcohol + NADP⁺ = an aldehyde + NADPH.
COFACTOR: Binds 1 zinc ion per subunit.
SUBUNIT: 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

X64841; CAA46053.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A32973; A32973.

3D structure databases

PDB

1BXZ; X-ray; 2.99 A; A/B/C/D=1-352.	[ExPASy / RCSB / EBI]
1YKF; X-ray; 2.50 A; A/B/C/D=1-352.	[ExPASy / RCSB / EBI]
2NVB; X-ray; 2.80 A; A/B/C/D=1-352.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BXZ; -.
1YKF; -.
2NVB; -.

ModBase

P14941.

Ontologies

GO:0008106;	Molecular function: alcohol dehydrogenase (NADP+) 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.

Other

P14941; -.

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

Keywords

3D-structure; Direct protein sequencing; Metal-binding; NADP; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 352`	`352`	`NADP-dependent alcohol dehydrogenase.`	`PRO_0000160749`
`METAL`	`37 37`		`Zinc; catalytic.`
`METAL`	`59 59`		`Zinc; catalytic.`
`METAL`	`150 150`		`Zinc; catalytic.`
`STRAND`	`2 8`	`7`
`STRAND`	`11 16`	`6`
`STRAND`	`27 35`	`9`
`HELIX`	`38 45`	`8`
`STRAND`	`53 56`	`4`
`STRAND`	`60 68`	`9`
`STRAND`	`80 83`	`4`
`STRAND`	`90 92`	`3`
`HELIX`	`93 96`	`4`
`HELIX`	`100 102`	`3`
`TURN`	`106 109`	`4`
`TURN`	`112 114`	`3`
`STRAND`	`121 128`	`8`
`HELIX`	`129 132`	`4`
`HELIX`	`142 145`	`4`
`TURN`	`146 150`	`5`
`HELIX`	`151 161`	`11`
`STRAND`	`170 173`	`4`
`HELIX`	`177 187`	`11`
`TURN`	`188 190`	`3`
`STRAND`	`192 197`	`6`
`HELIX`	`201 210`	`10`
`STRAND`	`213 216`	`4`
`HELIX`	`218 220`	`3`
`HELIX`	`223 230`	`8`
`TURN`	`231 233`	`3`
`STRAND`	`236 241`	`6`
`HELIX`	`248 255`	`8`
`STRAND`	`256 264`	`9`
`STRAND`	`270 272`	`3`
`TURN`	`278 285`	`8`
`STRAND`	`289 293`	`5`
`HELIX`	`299 310`	`12`
`HELIX`	`316 319`	`4`
`STRAND`	`320 326`	`7`
`HELIX`	`328 338`	`11`
`STRAND`	`345 350`	`6`

Sequence information

Length: 352 AA [This is the length of the unprocessed precursor]

Molecular weight: 37647 Da [This is the MW of the unprocessed precursor]

CRC64: E124A5351AD55185 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKGFAMLSIG KVGWIEKEKP APGPFDAIVR PLAVAPCTSD IHTVFEGAIG ERHNMILGHE 

        70         80         90        100        110        120 
AVGEVVEVGS EVKDFKPGDR VVVPAITPDW RTSEVQRGYH QHSGGMLAGW KFSNVKDGVF 

       130        140        150        160        170        180 
GEFFHVNDAD MNLAHLPKEI PLEAAVMIPD MMTTGFHGAE LADIELGATV AVLGIGPVGL 

       190        200        210        220        230        240 
MAVAGAKLRG AGRIIAVGSR PVCVDAAKYY GATDIVNYKD GPIESQIMNL TEGKGVDAAI 

       250        260        270        280        290        300 
IAGGNADIMA TAVKIVKPGG TIANVNYFGE GEVLPVPRLE WGCGMAHKTI KGGLCPGGRL 

       310        320        330        340        350 
RMERLIDLVF YKRVDPSKLV THVFRGFDNI EKAFMLMKDK PKDLIKPVVI LA

P14941 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