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Q9WYQ4 (GLDA_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol dehydrogenase

Short name=GDH
Short name=GLDH
EC=1.1.1.6
Gene names
Name:gldA
Ordered Locus Names:TM_0423
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processGlycerol metabolism
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanaerobic glycerol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionglycerol dehydrogenase [NAD+] activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Glycerol dehydrogenase
PRO_0000350665

Regions

Nucleotide binding92 – 965NAD By similarity
Nucleotide binding114 – 1174NAD By similarity

Sites

Metal binding1691Zinc; catalytic
Metal binding2521Zinc; catalytic
Metal binding2691Zinc; catalytic
Binding site371NAD By similarity
Binding site1191Substrate Probable
Binding site1231NAD By similarity
Binding site1251NAD; via carbonyl oxygen By similarity
Binding site1291NAD By similarity
Binding site1691Substrate Probable
Binding site2521Substrate Probable
Binding site2691Substrate Probable

Secondary structure

..................................................... 364
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WYQ4 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: B44E20CACC6F1582

FASTA36439,692
        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 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD35508.1.
PIRG72378.
RefSeqNP_228233.1. NC_000853.1.
YP_007976770.1. NC_021214.1.
YP_008990607.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KQ3X-ray1.50A1-364[»]
ProteinModelPortalQ9WYQ4.
SMRQ9WYQ4. Positions 1-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0423.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35508; AAD35508; TM_0423.
GeneID897429.
KEGGtma:TM0423.
tmi:THEMA_02610.
tmm:Tmari_0420.
PATRIC23935729. VBITheMar51294_0428.

Phylogenomic databases

eggNOGCOG0371.
KOK00005.
OMAYFEARAN.
OrthoDBEOG67432X.

Enzyme and pathway databases

UniPathwayUPA00617; UER00668.

Family and domain databases

InterProIPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
IPR016205. Glycerol_DH.
[Graphical view]
PfamPF00465. Fe-ADH. 1 hit.
[Graphical view]
PIRSFPIRSF000112. Glycerol_dehydrogenase. 1 hit.
PROSITEPS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9WYQ4.

Entry information

Entry nameGLDA_THEMA
AccessionPrimary (citable) accession number: Q9WYQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways