Reviewed, UniProtKB/Swiss-Prot P0A9S6 (GLDA_ECOL6)

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:	c4904

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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	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 – 367	367	Glycerol dehydrogenase		PRO_0000087829
Regions
	Nucleotide binding	94 – 98	5	NAD By similarity
	Nucleotide binding	116 – 119	4	NAD By similarity
Sites
	Metal binding	171	1	Zinc; catalytic By similarity
	Metal binding	254	1	Zinc; catalytic By similarity
	Metal binding	271	1	Zinc; catalytic By similarity
	Binding site	37	1	NAD By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	125	1	NAD By similarity
	Binding site	127	1	NAD; via carbonyl oxygen By similarity
	Binding site	131	1	NAD By similarity
	Binding site	171	1	Substrate By similarity
	Binding site	254	1	Substrate By similarity
	Binding site	271	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A9S6-1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: F6F3F275B4091F28	FASTA	367	38,712
	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

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN83332.1. Different initiation.
RefSeq	NP_756758.2.
3D structure databases
HSSP	HSSP built from PDB template 1KQ3 based on UniProtKB Q9WYQ4.
ModBase	Search...
Genome annotation databases
GeneID	1040105.
GenomeReviews	Gene locus c4904 in contig AE014075_GR.
KEGG	ecc:c4904.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A9S6.
OMA	KYIRFYQ.
Enzyme and pathway databases
BRENDA	1.1.1.6. 292881.
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_ECOL6

Accession

Primary (citable) accession number: P0A9S6
Secondary accession number(s): P32665, P78132

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	November 3, 2009
This is version 32 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)