| Tag | Content |
|---|
| CPLM ID | CPLM-006037 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | NADH-quinone oxidoreductase subunit F |
Protein Synonyms/Alias | NADH dehydrogenase I subunit F; NDH-1 subunit F; NUO6 |
Gene Name | nuoF |
Gene Synonyms/Alias | b2284; JW2279 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 21 | TWRLRDDKQPVWLDE | acetylation | [1] | | 40 | NGYEGARKALTGLSP | acetylation | [1] | | 55 | DEIVNQVKDAGLKGR | acetylation | [1, 2] | | 60 | QVKDAGLKGRGGAGF | acetylation | [1] | | 78 | LKWSLMPKDESMNIR | acetylation | [1] | | 200 | RRANPRSKPPFPATS | acetylation | [1] | | 257 | MGFSGRVKNPGLWEL | acetylation | [1] | | 286 | GGMRDGLKFKAWQPG | acetylation | [1] | | 366 | DGLPWSVKILRALER | acetylation | [1] | | 413 | EPLQSAIKYFREEFE | acetylation | [1] | | 424 | EEFEAGIKQPFSNTH | acetylation | [1] | | 442 | GIQPNLLKERW**** | 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] [2] 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] |
Functional Description | NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
Sequence Annotation | NP_BIND 61 70 NAD (By similarity).
NP_BIND 174 221 FMN (By similarity).
METAL 351 351 Iron-sulfur (4Fe-4S) (Potential).
METAL 354 354 Iron-sulfur (4Fe-4S) (Potential).
METAL 357 357 Iron-sulfur (4Fe-4S) (Potential).
METAL 398 398 Iron-sulfur (4Fe-4S) (Potential). |
Keyword | 4Fe-4S; Complete proteome; Direct protein sequencing; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Quinone; Reference proteome; Ubiquinone. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 445 AA |
Protein Sequence | MKNIIRTPET HPLTWRLRDD KQPVWLDEYR SKNGYEGARK ALTGLSPDEI VNQVKDAGLK 60
GRGGAGFSTG LKWSLMPKDE SMNIRYLLCN ADEMEPGTYK DRLLMEQLPH LLVEGMLISA 120
FALKAYRGYI FLRGEYIEAA VNLRRAIAEA TEAGLLGKNI MGTGFDFELF VHTGAGRYIC 180
GEETALINSL EGRRANPRSK PPFPATSGAW GKPTCVNNVE TLCNVPAILA NGVEWYQNIS 240
KSKDAGTKLM GFSGRVKNPG LWELPFGTTA REILEDYAGG MRDGLKFKAW QPGGAGTDFL 300
TEAHLDLPME FESIGKAGSR LGTALAMAVD HEINMVSLVR NLEEFFARES CGWCTPCRDG 360
LPWSVKILRA LERGEGQPGD IETLEQLCRF LGPGKTFCAH APGAVEPLQS AIKYFREEFE 420
AGIKQPFSNT HLINGIQPNL LKERW 445 |
Gene Ontology | GO:0045272; C:plasma membrane respiratory chain complex I; IDA:EcoCyc. GO:0051539; F:4 iron, 4 sulfur cluster binding; IMP:EcoCyc. GO:0010181; F:FMN binding; ISS:EcoCyc. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0051287; F:NAD binding; IMP:EcoCyc. GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. GO:0048038; F:quinone binding; IEA:UniProtKB-KW. GO:0009060; P:aerobic respiration; IMP:EcoCyc. |
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