CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002769
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Formate acetyltransferase 1 
Protein Synonyms/Alias
 Pyruvate formate-lyase 1 
Gene Name
 pflB 
Gene Synonyms/Alias
 pfl; b0903; JW0886 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
7*MSELNEKLATAWEGacetylation[1]
17TAWEGFTKGDWQNEVacetylation[2]
32NVRDFIQKNYTPYEGacetylation[2]
63DKVMEGVKLENRTHAacetylation[1, 2, 3]
92HDAGYINKQLEKIVGacetylation[2]
96YINKQLEKIVGLQTEacetylation[2]
107LQTEAPLKRALIPFGacetylation[2]
117LIPFGGIKMIEGSCKacetylation[1, 2, 3]
124KMIEGSCKAYNRELDacetylation[1, 2]
135RELDPMIKKIFTEYRacetylation[2]
136ELDPMIKKIFTEYRKacetylation[1, 2]
162PDILRCRKSGVLTGLacetylation[1, 2]
195YGIDYLMKDKLAQFTacetylation[1, 2, 3]
197IDYLMKDKLAQFTSLacetylation[1, 2]
235HRALGQMKEMAAKYGacetylation[1, 2]
293VYIERDLKAGKITEQacetylation[2]
312MVDHLVMKLRMVRFLacetylation[1, 2]
352DGRTLVTKNSFRFLNacetylation[2]
379MTILWSEKLPLNFKKacetylation[2]
385EKLPLNFKKFAAKVSacetylation[2]
441GARANLAKTMLYAINacetylation[2]
454INGGVDEKLKMQVGPacetylation[1, 2, 3]
456GGVDEKLKMQVGPKSacetylation[1, 2]
462LKMQVGPKSEPIKGDacetylation[1, 2]
467GPKSEPIKGDVLNYDacetylation[1, 2]
541ADSLSAIKYAKVKPIacetylation[2, 3]
544LSAIKYAKVKPIRDEacetylation[1]
588LVERFMKKIQKLHTYacetylation[2]
591RFMKKIQKLHTYRDAacetylation[1, 2, 3]
615TSNVVYGKKTGNTPDacetylation[2]
643PMHGRDQKGAVASLTacetylation[2]
654ASLTSVAKLPFAYAKacetylation[1, 2]
661KLPFAYAKDGISYTFacetylation[2]
677IVPNALGKDDEVRKTacetylation[2]
725DAMENPEKYPQLTIRacetylation[2]
745VRFNSLTKEQQQDVIacetylation[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]
 [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
  
Sequence Annotation
 DOMAIN 3 625 PFL.
 DOMAIN 632 760 Glycine radical.
 ACT_SITE 419 419 S-acetylcysteine intermediate.
 ACT_SITE 420 420 Cysteine radical intermediate.
 MOD_RES 63 63 N6-acetyllysine; alternate.
 MOD_RES 63 63 N6-succinyllysine; alternate.
 MOD_RES 107 107 N6-succinyllysine.
 MOD_RES 117 117 N6-acetyllysine; alternate.
 MOD_RES 117 117 N6-succinyllysine; alternate.
 MOD_RES 124 124 N6-acetyllysine; alternate.
 MOD_RES 124 124 N6-succinyllysine; alternate.
 MOD_RES 195 195 N6-acetyllysine; alternate.
 MOD_RES 195 195 N6-succinyllysine; alternate.
 MOD_RES 454 454 N6-acetyllysine; alternate.
 MOD_RES 454 454 N6-succinyllysine; alternate.
 MOD_RES 467 467 N6-succinyllysine.
 MOD_RES 541 541 N6-acetyllysine.
 MOD_RES 591 591 N6-acetyllysine.
 MOD_RES 654 654 N6-succinyllysine.
 MOD_RES 735 735 Glycine radical.  
Keyword
 3D-structure; Acetylation; Acyltransferase; Carbohydrate metabolism; Complete proteome; Cytoplasm; Direct protein sequencing; Glucose metabolism; Organic radical; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 760 AA 
Protein Sequence
MSELNEKLAT AWEGFTKGDW QNEVNVRDFI QKNYTPYEGD ESFLAGATEA TTTLWDKVME 60
GVKLENRTHA PVDFDTAVAS TITSHDAGYI NKQLEKIVGL QTEAPLKRAL IPFGGIKMIE 120
GSCKAYNREL DPMIKKIFTE YRKTHNQGVF DVYTPDILRC RKSGVLTGLP DAYGRGRIIG 180
DYRRVALYGI DYLMKDKLAQ FTSLQADLEN GVNLEQTIRL REEIAEQHRA LGQMKEMAAK 240
YGYDISGPAT NAQEAIQWTY FGYLAAVKSQ NGAAMSFGRT STFLDVYIER DLKAGKITEQ 300
EAQEMVDHLV MKLRMVRFLR TPEYDELFSG DPIWATESIG GMGLDGRTLV TKNSFRFLNT 360
LYTMGPSPEP NMTILWSEKL PLNFKKFAAK VSIDTSSLQY ENDDLMRPDF NNDDYAIACC 420
VSPMIVGKQM QFFGARANLA KTMLYAINGG VDEKLKMQVG PKSEPIKGDV LNYDEVMERM 480
DHFMDWLAKQ YITALNIIHY MHDKYSYEAS LMALHDRDVI RTMACGIAGL SVAADSLSAI 540
KYAKVKPIRD EDGLAIDFEI EGEYPQFGNN DPRVDDLAVD LVERFMKKIQ KLHTYRDAIP 600
TQSVLTITSN VVYGKKTGNT PDGRRAGAPF GPGANPMHGR DQKGAVASLT SVAKLPFAYA 660
KDGISYTFSI VPNALGKDDE VRKTNLAGLM DGYFHHEASI EGGQHLNVNV MNREMLLDAM 720
ENPEKYPQLT IRVSGYAVRF NSLTKEQQQD VITRTFTQSM 760 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0008861; F:formate C-acetyltransferase activity; IDA:EcoCyc.
 GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
 GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. 
Interpro
 IPR005949; Form_AcTrfase.
 IPR019777; Form_AcTrfase_GR_CS.
 IPR001150; Gly_radical.
 IPR004184; PFL_dom. 
Pfam
 PF01228; Gly_radical
 PF02901; PFL 
SMART
  
PROSITE
 PS00850; GLY_RADICAL_1
 PS51149; GLY_RADICAL_2
 PS51554; PFL 
PRINTS