[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/21.23.5408; PubMed=8265357 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.; "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."; Nucleic Acids Res. 21:5408-5417(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[4]	FUNCTION, CHARACTERIZATION, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, AND PH DEPENDENCE. PubMed=40950 [NCBI, ExPASy, EBI, Israel, Japan] Tang C.-T., Ruch F.E. Jr., Lin E.C.C.; "Purification and properties of a nicotinamide adenine dinucleotide-linked dehydrogenase that serves an Escherichia coli mutant for glycerol catabolism."; J. Bacteriol. 140:182-187(1979).
[5]	FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION. PubMed=8132480 [NCBI, ExPASy, EBI, Israel, Japan] Truniger V., Boos W.; "Mapping and cloning of gldA, the structural gene of the Escherichia coli glycerol dehydrogenase."; J. Bacteriol. 176:1796-1800(1994).
[6]	FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, AND ROLE IN DIHYDROXYACETONE METABOLISM. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1111/j.1574-6968.2007.01032.x; PubMed=18179582 [NCBI, ExPASy, EBI, Israel, Japan] Subedi K.P., Kim I., Kim J., Min B., Park C.; "Role of GldA in dihydroxyacetone and methylglyoxal metabolism of Escherichia coli K12."; FEMS Microbiol. Lett. 279:180-187(2008).
[7]	ROLE IN ANAEROBIC FERMENTATION OF GLYCEROL. DOI=10.1016/j.ymben.2008.05.001; PubMed=18632294 [NCBI, ExPASy, EBI, Israel, Japan] Gonzalez R., Murarka A., Dharmadi Y., Yazdani S.S.; "A new model for the anaerobic fermentation of glycerol in enteric bacteria: trunk and auxiliary pathways in Escherichia coli."; Metab. Eng. 10:234-245(2008).

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. In E.coli, an important role of gldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively.
CATALYTIC ACTIVITY: Glycerol + NAD⁺ = glycerone + NADH.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
ENZYME REGULATION: Inhibited by Cu(2+).

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=0.30 mM for dihydroxyacetone (at 25 degrees Celsius and pH 7);
	K_M=0.85 mM for glycolaldehyde (at 25 degrees Celsius and pH 7);
	K_M=0.50 mM for methylglyoxal (at 25 degrees Celsius and pH 7);
	K_M=56 mM for glycerol (at 25 degrees Celsius and pH 7);
	Note=The catalytic efficiency of the reverse reaction (dihydroxyacetone reduction) is more than 100-fold higher than that of the forward direction (glycerol oxidation);
pH dependence:	Optimum pH is 5.5-6.0 for dihydroxyacetone reduction and 9.5- 10.0 for glycerol oxidation;

PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 1/2 .
SUBUNIT: Homodimer and homooctamer.
DEVELOPMENTAL STAGE: Expression is higher during stationary phase than during logarithmic growth.
INDUCTION: Full expression of gldA is achieved by induction with hydroxyacetone and stationary-phase growth conditions.
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

U00006; AAC43051.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76927.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77365.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D65201; D65201.

RefSeq

AP_003864.1; -.
NP_418380.4; -.

3D structure databases

HSSP

Q9WYQ4; 1KQ3. [HSSP ENTRY / PDB]

ModBase

P0A9S5.

Enzyme and pathway databases

BioCyc

EcoCyc:GLYCDEH-MON; -.
MetaCyc:GLYCDEH-MON; -.

Organism-specific databases

EchoBASE

EB1849; -.

EcoGene

EG11904; gldA.

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.

Genome annotation databases

GeneID

948440; -.

GenomeReviews

AP009048_GR; JW5556.
U00096_GR; b3945.

KEGG

ecj:JW5556; -.
eco:b3945; -.

Phylogenomic databases

HOGENOM

P0A9S5; -.

Genome annotation databases

CMR

P0A9S5; b3945.

Other

ProtoNet

P0A9S5.

UniRef

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

Keywords

Complete proteome; Glycerol metabolism; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 367`	`367`	`Glycerol dehydrogenase.`	`PRO_0000087828`
`NP_BIND`	`94 98`	`5`	`NAD (By similarity).`
`NP_BIND`	`116 119`	`4`	`NAD (By similarity).`
`METAL`	`171 171`		`Zinc; catalytic (By similarity).`
`METAL`	`254 254`		`Zinc; catalytic (By similarity).`
`METAL`	`271 271`		`Zinc; catalytic (By similarity).`
`BINDING`	`37 37`		`NAD (By similarity).`
`BINDING`	`121 121`		`Substrate (By similarity).`
`BINDING`	`125 125`		`NAD (By similarity).`
`BINDING`	`127 127`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`131 131`		`NAD (By similarity).`
`BINDING`	`171 171`		`Substrate (By similarity).`
`BINDING`	`254 254`		`Substrate (By similarity).`
`BINDING`	`271 271`		`Substrate (By similarity).`

Sequence information

Length: 367 AA [This is the length of the unprocessed precursor]

Molecular weight: 38712 Da [This is the MW of the unprocessed precursor]

CRC64: F6F3F275B4091F28 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDRIIQSPGK YIQGADVINR LGEYLKPLAE RWLVVGDKFV LGFAQSTVEK SFKDAGLVVE 

        70         80         90        100        110        120 
IAPFGGECSQ NEIDRLRGIA ETAQCGAILG IGGGKTLDTA KALAHFMGVP VAIAPTIAST 

       130        140        150        160        170        180 
DAPCSALSVI YTDEGEFDRY LLLPNNPNMV IVDTKIVAGA PARLLAAGIG DALATWFEAR 

       190        200        210        220        230        240 
ACSRSGATTM AGGKCTQAAL ALAELCYNTL LEEGEKAMLA AEQHVVTPAL ERVIEANTYL 

       250        260        270        280        290        300 
SGVGFESGGL AAAHAVHNGL TAIPDAHHYY HGEKVAFGTL TQLVLENAPV EEIETVAALS 

       310        320        330        340        350        360 
HAVGLPITLA QLDIKEDVPA KMRIVAEAAC AEGETIHNMP GGATPDQVYA ALLVADQYGQ 


RFLQEWE

P0A9S5 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