[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=DSM 2334 / Var. Non-diastaticus; DOI=10.1016/0378-1119(92)90438-U; PubMed=1339360 [NCBI, ExPASy, EBI, Israel, Japan] Mallinder P.R., Pritchard A., Moir A.; "Cloning and characterization of a gene from Bacillus stearothermophilus var. non-diastaticus encoding a glycerol dehydrogenase."; Gene 110:9-16(1992).
[2]	PROTEIN SEQUENCE OF 84-103, AND MUTAGENESIS OF LYS-97. DOI=10.1016/0167-4838(93)90010-O; PubMed=8399385 [NCBI, ExPASy, EBI, Israel, Japan] Paine L.J., Perry N., Popplewell A.G., Gore M.G., Atkinson T.; "The identification of a lysine residue reactive to pyridoxal-5-phosphate in the glycerol dehydrogenase from the thermophile Bacillus stearothermophilus."; Biochim. Biophys. Acta 1202:235-243(1993).
[3]	FUNCTION, COFACTOR, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES. PubMed=2493267 [NCBI, ExPASy, EBI, Israel, Japan] Spencer P., Bown K.J., Scawen M.D., Atkinson T., Gore M.G.; "Isolation and characterisation of the glycerol dehydrogenase from Bacillus stearothermophilus."; Biochim. Biophys. Acta 994:270-279(1989).
[4]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT CYS-305 IN COMPLEXES WITH ZINC; NAD AND SUBSTRATE, DOMAIN, COFACTOR, SUBUNIT, AND MUTAGENESIS OF SER-305. PubMed=11566129 [NCBI, ExPASy, EBI, Israel, Japan] Ruzheinikov S.N., Burke J., Sedelnikova S., Baker P.J., Taylor R., Bullough P.A., Muir N.M., Gore M.G., Rice D.W.; "Glycerol dehydrogenase: structure, specificity, and mechanism of a family III polyol dehydrogenase."; Structure 9:789-802(2001).

Comments

FUNCTION: Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. Is also able to use various diols as substrates, such as propan-1,2-diol, butan-2,3-diol, ethan-1,2-diol, and 3-mercapto-1,2-dihydroxypropane.
CATALYTIC ACTIVITY: Glycerol + NAD⁺ = glycerone + NADH.
COFACTOR: Binds 1 zinc ion per subunit.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=3.8 mM for glycerol;
K_M=121 µM for NAD⁺;
pH dependence: Optimum pH is 6.0-8.5;
PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 1/2 .
SUBUNIT: Homooctamer.
DOMAIN: Consists of two domains that are separated by a deep cleft, in which the Zn(2+) ion is bound.
SIMILARITY: Belongs to the iron-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

M65289; AAA22477.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JQ1474; JQ1474.

3D structure databases

PDB

1JPU; X-ray; 1.80 A; A=1-370.	[ExPASy / RCSB / EBI]
1JQ5; X-ray; 1.70 A; A=1-370.	[ExPASy / RCSB / EBI]
1JQA; X-ray; 2.05 A; A=1-370.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1JPU; -.
1JQ5; -.
1JQA; -.

ModBase

P32816.

Ontologies

GO:0008888;	Molecular function: glycerol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006071;	Biological process: glycerol metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001670; Fe_AlcDHase.
IPR016205; Glycerol_DH.
Graphical view of domain structure.

Pfam

PF00465; Fe-ADH; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000112; Glycerol_dehydrogenase; 1.

PROSITE

PS00913; ADH_IRON_1; 1.
PS00060; ADH_IRON_2; 1.

ProtoNet

P32816.

Other

UniRef

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

Keywords

3D-structure; Direct protein sequencing; Glycerol metabolism; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 370`	`370`	`Glycerol dehydrogenase.`	`PRO_0000087826`
`NP_BIND`	`96 100`	`5`	`NAD.`
`NP_BIND`	`118 121`	`4`	`NAD.`
`METAL`	`173 173`		`Zinc; catalytic.`
`METAL`	`256 256`		`Zinc; catalytic.`
`METAL`	`274 274`		`Zinc; catalytic.`
`BINDING`	`39 39`		`NAD.`
`BINDING`	`123 123`		`Substrate.`
`BINDING`	`127 127`		`NAD.`
`BINDING`	`129 129`		`NAD; via carbonyl oxygen.`
`BINDING`	`133 133`		`NAD.`
`BINDING`	`173 173`		`Substrate.`
`BINDING`	`256 256`		`Substrate.`
`BINDING`	`274 274`		`Substrate.`
`MUTAGEN`	`97 97`		`K->H: Loss of activity.`
`MUTAGEN`	`305 305`		`S->C: No effect on affinity for substrates.`
`STRAND`	`5 8`	`4`
`STRAND`	`11 16`	`6`
`HELIX`	`19 22`	`4`
`HELIX`	`23 27`	`5`
`TURN`	`28 30`	`3`
`STRAND`	`32 38`	`7`
`HELIX`	`40 45`	`6`
`HELIX`	`47 56`	`10`
`STRAND`	`60 65`	`6`
`HELIX`	`72 85`	`14`
`STRAND`	`88 95`	`8`
`HELIX`	`96 109`	`14`
`STRAND`	`112 119`	`8`
`STRAND`	`128 130`	`3`
`STRAND`	`150 155`	`6`
`HELIX`	`156 160`	`5`
`HELIX`	`164 187`	`24`
`STRAND`	`194 196`	`3`
`HELIX`	`199 224`	`26`
`HELIX`	`230 250`	`21`
`HELIX`	`254 261`	`8`
`HELIX`	`262 264`	`3`
`HELIX`	`268 271`	`4`
`HELIX`	`274 288`	`15`
`HELIX`	`293 305`	`13`
`TURN`	`312 316`	`5`
`HELIX`	`322 332`	`11`
`HELIX`	`338 341`	`4`
`HELIX`	`347 365`	`19`

Sequence information

Length: 370 AA [This is the length of the unprocessed precursor]

Molecular weight: 39501 Da [This is the MW of the unprocessed precursor]

CRC64: E5D93264B1670F25 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAERVFISP AKYVQGKNVI TKIANYLEGI GNKTVVIADE IVWKIAGHTI VNELKKGNIA 

        70         80         90        100        110        120 
AEEVVFSGEA SRNEVERIAN IARKAEAAIV IGVGGGKTLD TAKAVADELD AYIVIVPTAA 

       130        140        150        160        170        180 
STDAPTSALS VIYSDDGVFE SYRFYKKNPD LVLVDTKIIA NAPPRLLASG IADALATWVE 

       190        200        210        220        230        240 
ARSVIKSGGK TMAGGIPTIA AEAIAEKCEQ TLFKYGKLAY ESVKAKVVTP ALEAVVEANT 

       250        260        270        280        290        300 
LLSGLGFESG GLAAAHAIHN GFTALEGEIH HLTHGEKVAF GTLVQLALEE HSQQEIERYI 

       310        320        330        340        350        360 
ELYLSLDLPV TLEDIKLKDA SREDILKVAK AATAEGETIH NAFNVTADDV ADAIFAADQY 

       370 
AKAYKEKHRK

P32816 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