CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003202
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycerol dehydrogenase 
Protein Synonyms/Alias
 GDH; GLDH 
Gene Name
 gldA 
Gene Synonyms/Alias
 b3945; JW5556 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
26NRLGEYLKPLAERWLacetylation[1]
50FAQSTVEKSFKDAGLacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively. 
Sequence Annotation
 NP_BIND 94 98 NAD (By similarity).
 NP_BIND 116 119 NAD (By similarity).
 METAL 171 171 Zinc; catalytic (By similarity).
 METAL 254 254 Zinc; catalytic (By similarity).
 METAL 271 271 Zinc; catalytic (By similarity).
 BINDING 37 37 NAD (By similarity).
 BINDING 121 121 Substrate (By similarity).
 BINDING 125 125 NAD (By similarity).
 BINDING 127 127 NAD; via carbonyl oxygen (By similarity).
 BINDING 131 131 NAD (By similarity).
 BINDING 171 171 Substrate (By similarity).
 BINDING 254 254 Substrate (By similarity).
 BINDING 271 271 Substrate (By similarity).  
Keyword
 Complete proteome; Direct protein sequencing; Glycerol metabolism; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 367 AA 
Protein Sequence
MDRIIQSPGK YIQGADVINR LGEYLKPLAE RWLVVGDKFV LGFAQSTVEK SFKDAGLVVE 60
IAPFGGECSQ NEIDRLRGIA ETAQCGAILG IGGGKTLDTA KALAHFMGVP VAIAPTIAST 120
DAPCSALSVI YTDEGEFDRY LLLPNNPNMV IVDTKIVAGA PARLLAAGIG DALATWFEAR 180
ACSRSGATTM AGGKCTQAAL ALAELCYNTL LEEGEKAMLA AEQHVVTPAL ERVIEANTYL 240
SGVGFESGGL AAAHAVHNGL TAIPDAHHYY HGEKVAFGTL TQLVLENAPV EEIETVAALS 300
HAVGLPITLA QLDIKEDVPA KMRIVAEAAC AEGETIHNMP GGATPDQVYA ALLVADQYGQ 360
RFLQEWE 367 
Gene Ontology
 GO:0019147; F:(R)-aminopropanol dehydrogenase activity; IDA:EcoCyc.
 GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IDA:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0019588; P:anaerobic glycerol catabolic process; IMP:EcoCyc.
 GO:0051596; P:methylglyoxal catabolic process; IMP:EcoCyc. 
Interpro
 IPR001670; ADH_Fe.
 IPR018211; ADH_Fe_CS.
 IPR016205; Glycerol_DH. 
Pfam
 PF00465; Fe-ADH 
SMART
  
PROSITE
 PS00913; ADH_IRON_1
 PS00060; ADH_IRON_2 
PRINTS