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Reviewed, UniProtKB/Swiss-Prot P45511 (GLDA_CITFR)

Last modified June 16, 2009. Version 47. 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: dhaD
OrganismCitrobacter freundii
Taxonomic identifier546 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter

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Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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. Exhibits a rather broad substrate specificity since it can also oxidize 1,2-propanediol and 2,3-butanediol and reduce dihydroxyacetone. Can not use NADP+ as an electron acceptor for the oxidation of glycerol.

Catalytic activity

Glycerol + NAD+ = glycerone + NADH.

Cofactor

Manganese.

Enzyme regulation

Inhibited by zinc.

Pathway

Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 1/2.

Subunit structure

Homohexamer.

Sequence similarities

Belongs to the iron-containing alcohol dehydrogenase family.

biophysicochemical properties

Kinetic parameters:

KM=1.27 mM for glycerol

KM=57 µM for NAD+

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Ontologies

Keywords
   Biological processGlycerol metabolism
   LigandManganese
Metal-binding
NAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
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

manganese 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_0000087827

Regions

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

Sites

Metal binding1711Manganese; catalytic By similarity
Metal binding2541Manganese; catalytic By similarity
Metal binding2711Manganese; 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
P45511-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: CB20076C0EE9DD8B

FASTA36539,019
        10         20         30         40         50         60 
MLKVIQSPAK YLQGPDASTL FGQYAKNLAD SFFVIADDFV MKLAGEKVLN GLHSHDISCH 

        70         80         90        100        110        120 
AERFNGECSH IEINRLIAIL KQHGCRGVVG IGGGKTLDTA KAIGYYQKLP VVVIPTIAST 

       130        140        150        160        170        180 
DAPTSALSVI YTEAGEFEEY LIYPKNPDMV VMDTAIIAKA PVRLLVAGMG DALSTWFEAK 

       190        200        210        220        230        240 
ACYDARATSM AGGQSTVAAL SLARLCYDTL LAEGEKARFA AQAGVVTDAL ERIVEANTYL 

       250        260        270        280        290        300 
SGIGFESSGL AGAHAIHNGF TILEECHHLY HGEKVAFGTL AQLVLQNSPM EEIETVLNFC 

       310        320        330        340        350        360 
QKVGLPVTLA EMGVKDDIDG KIMAVAKATC AEGETIHNMP FSVTPESVHA AILTADLLGQ 


QWLAR

« Hide

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References

[1]"Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii."
Daniel R., Stuertz K., Gottschalk G.
J. Bacteriol. 177:4392-4401(1995) [PubMed: 7635824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30, CHARACTERIZATION.
Strain: ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK.

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Cross-references

Sequence databases

U09771 Genomic DNA. Translation: AAB48844.1.

3D structure databases

HSSPHSSP built from PDB template 1JPU based on UniProtKB P32816.
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MON-4503.
BRENDA1.1.1.6. 2347.

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...

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Entry information

Entry nameGLDA_CITFR
AccessionPrimary (citable) accession number: P45511
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 47 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