Tag | Content |
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CPLM ID | CPLM-007191 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | NADP-dependent 3-hydroxy acid dehydrogenase YdfG |
Protein Synonyms/Alias | Malonic semialdehyde reductase |
Gene Name | ydfG |
Gene Synonyms/Alias | b1539; JW1532 |
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 | RFIQQGHKVIATGRR | acetylation | [1, 2] | 41 | QERLQELKDELGDNL | acetylation | [2] | 151 | GNVYGATKAFVRQFS | acetylation | [2] | 191 | EFSNVRFKGDDGKAE | acetylation | [2] | 196 | RFKGDDGKAEKTYQN | acetylation | [2] |
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Reference | [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] [2] 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 | Has a broad substrate specificity and is able to catalyze the reduction of the malonic semialdehyde to 3- hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimidine degradation since both are able to detoxify malonic semialdehyde. Also catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L- glycerate. Although usually assayed in vitro as an oxidase, YdfG is presumed to be a reductase in vivo. |
Sequence Annotation | NP_BIND 4 28 NADP (By similarity). ACT_SITE 147 147 Proton acceptor (By similarity). BINDING 134 134 Substrate (By similarity). |
Keyword | Complete proteome; Direct protein sequencing; NADP; Oxidoreductase; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 248 AA |
Protein Sequence | MIVLVTGATA GFGECITRRF IQQGHKVIAT GRRQERLQEL KDELGDNLYI AQLDVRNRAA 60 IEEMLASLPA EWCNIDILVN NAGLALGMEP AHKASVEDWE TMIDTNNKGL VYMTRAVLPG 120 MVERNHGHII NIGSTAGSWP YAGGNVYGAT KAFVRQFSLN LRTDLHGTAV RVTDIEPGLV 180 GGTEFSNVRF KGDDGKAEKT YQNTVALTPE DVSEAVWWVS TLPAHVNINT LEMMPVTQSY 240 AGLNVHRQ 248 |
Gene Ontology | GO:0035527; F:3-hydroxypropionate dehydrogenase (NADP+) activity; IDA:EcoCyc. GO:0031132; F:serine 3-dehydrogenase activity; IDA:EcoCyc. GO:0006212; P:uracil catabolic process; IDA:UniProtKB. |
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