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Reviewed, UniProtKB/Swiss-Prot P50173 (GLDA_PSEPU)

Last modified November 4, 2008. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glycerol dehydrogenase
      Short name=GLDH
      Short name=GDH
    EC=1.1.1.6
Gene names
Name: gldA
Synonyms: bedD
Encoded onPlasmid pHMT112
OrganismPseudomonas putida
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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Ontologies

Keywords

   Biological processGlycerol metabolism
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termPlasmid

Gene Ontology (GO)

   Biological processglycerol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglycerol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Glycerol dehydrogenase
PRO_0000087830

Regions

Nucleotide binding94 – 985NAD By similarity
Nucleotide binding116 – 1194NAD By similarity

Sites

Metal binding1711Zinc; catalytic By similarity
Metal binding2541Zinc; catalytic By similarity
Metal binding2711Zinc; catalytic By similarity
Binding site371NAD By similarity
Binding site1211Substrate By similarity
Binding site1251NAD By similarity
Binding site1271NAD; via carbonyl oxygen By similarity
Binding site1311NAD By similarity
Binding site1711Substrate By similarity
Binding site2541Substrate By similarity
Binding site2711Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
P50173-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D6AEAA16D52A8D47

FASTA36538,316
        10         20         30         40         50         60 
MDRAIQSPGK YVQGADALQR LGDYLKPLAD SWLVIADKFV LGFAEDTIRQ SLSKAGLAMD 

        70         80         90        100        110        120 
IVAFNGECSQ GEVDRLCQLA TQNGRSAIVG IGGGKTLDTA KAVAFFQKVP VAVAPTIAST 

       130        140        150        160        170        180 
DAPCSALSVL YTDEGEFDRY LMLPTNPALV VVDTAIVARA PARLLAAGIG DALATWFEAR 

       190        200        210        220        230        240 
AASRSSAATM AGGPATQTAL NLARFCYDTL LEEGEKAMLA VQAQVVTPAL ERIVEANTYL 

       250        260        270        280        290        300 
SGVGFESGGV AAAHAVHNGL TAVAETHHFY HGEKVAFGVL VQLALENASN AEMQEVMSLC 

       310        320        330        340        350        360 
HAVGLPITLA QLDITEDIPT KMRAVAELAC APGETIHNMP GGVTVEQVYG ALLVADQLGQ 


HFLEF

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References

[1]"Characterization and expression of the plasmid-borne bedD gene from Pseudomonas putida ML2, which codes for a NAD+-dependent cis-benzene dihydrodiol dehydrogenase."
Fong K.P.Y., Goh C.B.H., Tan H.M.
J. Bacteriol. 178:5592-5601(1996) [PubMed: 8824602] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ML2.

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Cross-references

Sequence databases

AF148496 Genomic DNA. Translation: AAC44426.1.

3D structure databases

HSSPHSSP built from PDB template 1KQ3 based on UniProtKB Q9WYQ4.
ModBaseSearch...

Family and domain databases

InterProIPR001670. Fe_AlcDHase.
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...

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Entry information

Entry nameGLDA_PSEPU
AccessionPrimary (citable) accession number: P50173
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 4, 2008
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents