| Tag | Content |
|---|
| CPLM ID | CPLM-001748 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Fumarate reductase flavoprotein subunit |
Protein Synonyms/Alias | |
Gene Name | frdA |
Gene Synonyms/Alias | b4154; JW4115 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 121 | VRRFGGMKIERTWFA | acetylation | [1, 2] | | 258 | EGGILVNKNGYRYLQ | acetylation | [2] | | 281 | PLGEPKNKYMELGPR | acetylation | [1, 2] | | 337 | PFICELAKAYVGVDP | acetylation | [1, 2] | | 346 | YVGVDPVKEPIPVRP | acetylation | [2] | | 373 | QNCETRIKGLFAVGE | acetylation | [1] | | 438 | AGVEQRLKDLVNQDG | acetylation | [2] | | 475 | RTPELMQKTIDKLAE | acetylation | [2] | | 479 | LMQKTIDKLAELQER | acetylation | [2] | | 550 | RDDVNFLKHTLAFRD | acetylation | [2] | | 590 | GEADAADKAEAANKK | acetylation | [2] |
|
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 | Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. |
Sequence Annotation | NP_BIND 9 23 FAD (Potential).
ACT_SITE 233 233
ACT_SITE 249 249
MOD_RES 45 45 Tele-8alpha-FAD histidine. |
Keyword | 3D-structure; Complete proteome; Electron transport; FAD; Flavoprotein; Oxidoreductase; Reference proteome; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 602 AA |
Protein Sequence | MQTFQADLAI VGAGGAGLRA AIAAAQANPN AKIALISKVY PMRSHTVAAE GGSAAVAQDH 60
DSFEYHFHDT VAGGDWLCEQ DVVDYFVHHC PTEMTQLELW GCPWSRRPDG SVNVRRFGGM 120
KIERTWFAAD KTGFHMLHTL FQTSLQFPQI QRFDEHFVLD ILVDDGHVRG LVAMNMMEGT 180
LVQIRANAVV MATGGAGRVY RYNTNGGIVT GDGMGMALSH GVPLRDMEFV QYHPTGLPGS 240
GILMTEGCRG EGGILVNKNG YRYLQDYGMG PETPLGEPKN KYMELGPRDK VSQAFWHEWR 300
KGNTISTPRG DVVYLDLRHL GEKKLHERLP FICELAKAYV GVDPVKEPIP VRPTAHYTMG 360
GIETDQNCET RIKGLFAVGE CSSVGLHGAN RLGSNSLAEL VVFGRLAGEQ ATERAATAGN 420
GNEAAIEAQA AGVEQRLKDL VNQDGGENWA KIRDEMGLAM EEGCGIYRTP ELMQKTIDKL 480
AELQERFKRV RITDTSSVFN TDLLYTIELG HGLNVAECMA HSAMARKESR GAHQRLDEGC 540
TERDDVNFLK HTLAFRDADG TTRLEYSDVK ITTLPPAKRV YGGEADAADK AEAANKKEKA 600
NG 602 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:EcoCyc. GO:0016020; C:membrane; IDA:UniProtKB. GO:0009055; F:electron carrier activity; IDA:EcoCyc. GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc. GO:0000104; F:succinate dehydrogenase activity; IEA:EC. GO:0009061; P:anaerobic respiration; IMP:EcoCyc. GO:0001539; P:ciliary or flagellar motility; IMP:EcoCyc. GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. GO:0006113; P:fermentation; IMP:EcoCyc. GO:0009296; P:flagellum assembly; IMP:EcoCyc. GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki. |
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Pfam | |
SMART | |
PROSITE | |
PRINTS | |