| Tag | Content |
|---|
| CPLM ID | CPLM-010298 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Probable pyridine nucleotide-disulfide oxidoreductase YkgC |
Protein Synonyms/Alias | |
Gene Name | ykgC |
Gene Synonyms/Alias | b0304; JW5040 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 24 | TLAVTLAKAGWRVAL | acetylation | [1] | | 81 | VVNFLRNKNFHNLAD | acetylation | [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 | |
Sequence Annotation | NP_BIND 33 43 FAD (By similarity).
ACT_SITE 426 426 Proton acceptor (By similarity).
DISULFID 43 48 Redox-active (By similarity). |
Keyword | Complete proteome; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 441 AA |
Protein Sequence | MNKYQAVIIG FGKAGKTLAV TLAKAGWRVA LIEQSNAMYG GTCINIGCIP TKTLVHDAQQ 60
HTDFVRAIQR KNEVVNFLRN KNFHNLADMP NIDVIDGQAE FINNHSLRVH RPEGNLEIHG 120
EKIFINTGAQ TVVPPIPGIT TTPGVYDSTG LLNLKELPGH LGILGGGYIG VEFASMFANF 180
GSKVTILEAA SLFLPREDRD IADNIATILR DQGVDIILNA HVERISHHEN QVQVHSEHAQ 240
LAVDALLIAS GRQPATASLH PENAGIAVNE RGAIVVDKRL HTTADNIWAM GDVTGGLQFT 300
YISLDDYRIV RDELLGEGKR STDDRKNVPY SVFMTPPLSR VGMTEEQARE SGADIQVVTL 360
PVAAIPRARV MNDTRGVLKA IVDNKTQRML GASLLCVDSH EMINIVKMVM DAGLPYSILR 420
DQIFTHPSMS ESLNDLFSLV K 441 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:InterPro. GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro. GO:0045454; P:cell redox homeostasis; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |