Tag | Content |
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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 |
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26 | NRLGEYLKPLAERWL | acetylation | [1] | 50 | FAQSTVEKSFKDAGL | acetylation | [1] |
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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. |
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