Reviewed, UniProtKB/Swiss-Prot Q9WYQ4 (GLDA_THEMA)

Names and origin

Protein names

Recommended name:
    Glycerol dehydrogenase
      Short name=GLDH
      Short name=GDH
    EC=1.1.1.6

Gene names

Name:	gldA
Ordered Locus Names:	TM_0423

Organism

Thermotoga maritima [Complete proteome] [HAMAP]

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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 By similarity.
Catalytic activity	Glycerol + NAD+ = glycerone + NADH.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 1/2.
Sequence similarities	Belongs to the iron-containing alcohol dehydrogenase family.

Ontologies

Keywords
Biological process	Glycerol metabolism
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glycerol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	glycerol dehydrogenase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 364	364	Glycerol dehydrogenase		PRO_0000350665
Regions
	Nucleotide binding	92 – 96	5	NAD By similarity
	Nucleotide binding	114 – 117	4	NAD By similarity
Sites
	Metal binding	169	1	Zinc; catalytic
	Metal binding	252	1	Zinc; catalytic
	Metal binding	269	1	Zinc; catalytic
	Binding site	37	1	NAD By similarity
	Binding site	119	1	Substrate Probable
	Binding site	123	1	NAD By similarity
	Binding site	125	1	NAD; via carbonyl oxygen By similarity
	Binding site	129	1	NAD By similarity
	Binding site	169	1	Substrate Probable
	Binding site	252	1	Substrate Probable
	Binding site	269	1	Substrate Probable

Sequences

	Sequence		Length	Mass (Da)
	Q9WYQ4-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: B44E20CACC6F1582	FASTA	364	39,692
	10 20 30 40 50 60 MITTTIFPGR YVQGAGAINI LEEELSRFGE RAFVVIDDFV DKNVLGENFF SSFTKVRVNK 70 80 90 100 110 120 QIFGGECSDE EIERLSGLVE EETDVVVGIG GGKTLDTAKA VAYKLKKPVV IVPTIASTDA 130 140 150 160 170 180 PCSALSVIYT PNGEFKRYLF LPRNPDVVLV DTEIVAKAPA RFLVAGMGDA LATWFEAESC 190 200 210 220 230 240 KQKYAPNMTG RLGSMTAYAL ARLCYETLLE YGVLAKRSVE EKSVTPALEK IVEANTLLSG 250 260 270 280 290 300 LGFESGGLAA AHAIHNGLTV LENTHKYLHG EKVAIGVLAS LFLTDKPRKM IEEVYSFCEE 310 320 330 340 350 360 VGLPTTLAEI GLDGVSDEDL MKVAEKACDK NETIHNEPQP VTSKDVFFAL KAADRYGRMR KNLT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline." Lesley S.A., Kuhn P., Godzik A., Deacon A.M., Mathews I., Kreusch A., Spraggon G., Klock H.E., McMullan D., Shin T., Vincent J., Robb A., Brinen L.S., Miller M.D., McPhillips T.M., Miller M.A., Scheibe D., Canaves J.M. , Guda C., Jaroszewski L., Selby T.L., Elsliger M.-A., Wooley J., Taylor S.S., Hodgson K.O., Wilson I.A., Schultz P.G., Stevens R.C. Proc. Natl. Acad. Sci. U.S.A. 99:11664-11669(2002) [PubMed: 12193646] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH ZINC AND SUBSTRATE ANALOG. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE000512 Genomic DNA. Translation: AAD35508.1.

PIR

G72378.

RefSeq

NP_228233.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KQ3	X-ray	1.50	A	1-364	[»]

ModBase

Search...

Genome annotation databases

GeneID

897429.

GenomeReviews

Gene locus TM_0423 in contig AE000512_GR.

KEGG

tma:TM0423.

NMPDR

fig|243274.1.peg.417.

TIGR

TM_0423.

Phylogenomic databases

HOGENOM

Q9WYQ4.

OMA

Q9WYQ4. ADWELAH.

Enzyme and pathway databases

BioCyc

TMAR243274:TM0423-MONOMER.

Family and domain databases

InterPro

IPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
IPR016205. Glycerol_DH.
[Graphical view]

Pfam

PF00465. Fe-ADH. 1 hit.
[Graphical view]

PIRSF

PIRSF000112. Glycerol_dehydrogenase. 1 hit.

PROSITE

PS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLDA_THEMA

Accession

Primary (citable) accession number: Q9WYQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)