CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003322
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fumarate hydratase class I, aerobic 
Protein Synonyms/Alias
 Fumarase 
Gene Name
 fumA 
Gene Synonyms/Alias
 b1612; JW1604 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
4****MSNKPFHYQAPacetylation[1]
15YQAPFPLKKDDTEYYacetylation[1, 2]
116GTAIIVGKKGQRVWTacetylation[1, 2]
156NAPLDMYKEVNTGTNacetylation[1]
179AVDGDEYKFLCIAKGacetylation[1]
192KGGGSANKTYLYQETacetylation[1, 2, 3]
200TYLYQETKALLTPGKacetylation[1]
207KALLTPGKLKNYLVEacetylation[1]
215LKNYLVEKMRTLGTAacetylation[1]
251TVKLASAKYYDELPTacetylation[1]
337RQGIWIEKLEHNPGKacetylation[1]
344KLEHNPGKYIPEELRacetylation[1]
368VDLNRPMKEILAQLSacetylation[1]
399GRDIAHAKLKERMDNacetylation[1]
415EGLPQYIKDHPIYYAacetylation[1]
426IYYAGPAKTPEGYASacetylation[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]
 [3] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842] 
Functional Description
 It functions as an aerobic enzyme in the citric acid cycle. It accounts for about 80% of the fumarase activity when the bacteria grows aerobically. 
Sequence Annotation
 ACT_SITE 397 397 Potential.
 METAL 318 318 Iron-sulfur (4Fe-4S) (By similarity).
 BINDING 463 463 Substrate (Potential).  
Keyword
 4Fe-4S; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 548 AA 
Protein Sequence
MSNKPFHYQA PFPLKKDDTE YYLLTSEHVS VSEFEGQEIL KVAPEALTLL ARQAFHDASF 60
MLRPAHQQQV ADILRDPEAS ENDKYVALQF LRNSDIAAKG VLPTCQDTGT AIIVGKKGQR 120
VWTGGGDEAA LARGVYNTYI EDNLRYSQNA PLDMYKEVNT GTNLPAQIDL YAVDGDEYKF 180
LCIAKGGGSA NKTYLYQETK ALLTPGKLKN YLVEKMRTLG TAACPPYHIA FVIGGTSAET 240
NLKTVKLASA KYYDELPTEG NEHGQAFRDV ELEKELLIEA QNLGLGAQFG GKYFAHDIRV 300
IRLPRHGASC PVGMGVSCSA DRNIKAKINR QGIWIEKLEH NPGKYIPEEL RKAGEGEAVR 360
VDLNRPMKEI LAQLSQYPVS TRLSLNGTII VGRDIAHAKL KERMDNGEGL PQYIKDHPIY 420
YAGPAKTPEG YASGSLGPTT AGRMDSYVDQ LQAQGGSMIM LAKGNRSQQV TDACKKHGGF 480
YLGSIGGPAA VLAQGSIKSL ECVEYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIQL 540
TQCTRCVK 548 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
 GO:0004333; F:fumarate hydratase activity; IDA:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0050163; F:oxaloacetate tautomerase activity; IDA:EcoCyc.
 GO:0006099; P:tricarboxylic acid cycle; IMP:EcoCyc. 
Interpro
 IPR004646; Fe-S_hydro-lyase_TtdA-typ_cat.
 IPR004647; Fe-S_hydro-lyase_TtdB-typ_cat.
 IPR011167; Fe_dep_fumarate_hydratase.
 IPR020557; Fumarate_lyase_CS. 
Pfam
 PF05681; Fumerase
 PF05683; Fumerase_C 
SMART
  
PROSITE
 PS00163; FUMARATE_LYASES 
PRINTS