| Tag | Content |
|---|
| CPLM ID | CPLM-004228 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Fumarate hydratase class I, anaerobic |
Protein Synonyms/Alias | Fumarase |
Gene Name | fumB |
Gene Synonyms/Alias | b4122; JW4083 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 179 | AVDGDEYKFLCVAKG | acetylation | [1] | | 215 | LKNFLVEKMRTLGTA | acetylation | [1] | | 408 | KELIDAGKELPQYIK | 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 | It functions in the generation of fumarate for use as an anaerobic electron acceptor. |
Sequence Annotation | ACT_SITE 397 397 Potential.
METAL 318 318 Iron-sulfur (4Fe-4S) (By similarity).
BINDING 463 463 Substrate (Potential).
MOD_RES 192 192 N6-acetyllysine. |
Keyword | 4Fe-4S; Acetylation; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome; Tricarboxylic acid cycle. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 548 AA |
Protein Sequence | MSNKPFIYQA PFPMGKDNTE YYLLTSDYVS VADFDGETIL KVEPEALTLL AQQAFHDASF 60
MLRPAHQKQV AAILHDPEAS ENDKYVALQF LRNSEIAAKG VLPTCQDTGT AIIVGKKGQR 120
VWTGGGDEET LSKGVYNTYI EDNLRYSQNA ALDMYKEVNT GTNLPAQIDL YAVDGDEYKF 180
LCVAKGGGSA NKTYLYQETK ALLTPGKLKN FLVEKMRTLG TAACPPYHIA FVIGGTSAET 240
NLKTVKLASA HYYDELPTEG NEHGQAFRDV QLEQELLEEA QKLGLGAQFG GKYFAHDIRV 300
IRLPRHGASC PVGMGVSCSA DRNIKAKINR EGIWIEKLEH NPGQYIPQEL RQAGEGEAVK 360
VDLNRPMKEI LAQLSQYPVS TRLSLTGTII VGRDIAHAKL KELIDAGKEL PQYIKDHPIY 420
YAGPAKTPAG YPSGSLGPTT AGRMDSYVDL LQSHGGSMIM LAKGNRSQQV TDACHKHGGF 480
YLGSIGGPAA VLAQQSIKHL ECVAYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIVN 540
KQCANCTK 548 |
Gene Ontology | GO:0005829; C:cytosol; IDA:UniProtKB. GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. GO:0047808; F:D(-)-tartrate dehydratase activity; IMP:EcoCyc. GO:0004333; F:fumarate hydratase activity; IDA:EcoCyc. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0042710; P:biofilm formation; IMP:EcoCyc. GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki. GO:0006099; P:tricarboxylic acid cycle; IGI:EcoCyc. |
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