CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005589
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acetyl-coenzyme A synthetase 
Protein Synonyms/Alias
 AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme 
Gene Name
 acs 
Gene Synonyms/Alias
 yfaC; b4069; JW4030 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
50GKILDWIKPYQKVKNacetylation[1]
106GDDASQSKHISYKELacetylation[1]
111QSKHISYKELHRDVCacetylation[1]
130TLLELGIKKGDVVAIacetylation[1]
200GRSIPLKKNVDDALKacetylation[1]
207KNVDDALKNPNVTSVacetylation[1]
221VEHVVVLKRTGGKIDacetylation[1]
370ALMAEGDKAIEGTDRacetylation[1]
400EAWEWYWKKIGNEKCacetylation[1]
609LPKTRSGKIMRRILRacetylation[2, 3]
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] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [3] 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
 Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the firs thalf reaction, Acs combines acetate with ATP to form acetyl- adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. 
Sequence Annotation
 REGION 191 194 Coenzyme A (By similarity).
 REGION 411 416 Substrate binding (By similarity).
 ACT_SITE 517 517 By similarity.
 METAL 537 537 Magnesium; via carbonyl oxygen (By
 METAL 539 539 Magnesium; via carbonyl oxygen (By
 METAL 542 542 Magnesium; via carbonyl oxygen (By
 BINDING 311 311 Coenzyme A (By similarity).
 BINDING 335 335 Coenzyme A (By similarity).
 BINDING 387 387 Substrate; via amide nitrogen (By
 BINDING 500 500 Substrate (By similarity).
 BINDING 515 515 Substrate (By similarity).
 BINDING 523 523 Coenzyme A (By similarity).
 BINDING 526 526 Substrate (By similarity).
 BINDING 584 584 Coenzyme A (By similarity).
 MOD_RES 609 609 N6-acetyllysine.  
Keyword
 Acetylation; ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 652 AA 
Protein Sequence
MSQIHKHTIP ANIADRCLIN PQQYEAMYQQ SINVPDTFWG EQGKILDWIK PYQKVKNTSF 60
APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DASQSKHISY KELHRDVCRF 120
ANTLLELGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSNS 180
RLVITSDEGV RAGRSIPLKK NVDDALKNPN VTSVEHVVVL KRTGGKIDWQ EGRDLWWHDL 240
VEQASDQHQA EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAALTFK YVFDYHPGDI 300
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMAQVVDKHQ VNILYTAPTA 360
IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK KIGNEKCPVV DTWWQTETGG 420
FMITPLPGAT ELKAGSATRP FFGVQPALVD NEGNPLEGAT EGSLVITDSW PGQARTLFGD 480
HERFEQTYFS TFKNMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP 540
KIAEAAVVGI PHNIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD 600
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM PS 652 
Gene Ontology
 GO:0003987; F:acetate-CoA ligase activity; IDA:EcoCyc.
 GO:0016208; F:AMP binding; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0050218; F:propionate-CoA ligase activity; IDA:EcoCyc.
 GO:0045733; P:acetate catabolic process; IMP:EcoCyc.
 GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:HAMAP.
 GO:0006935; P:chemotaxis; IEA:HAMAP. 
Interpro
 IPR011904; Ac_CoA_lig.
 IPR024597; Acyl-CoA_synth_DUF3448.
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig.
 IPR025110; DUF4009. 
Pfam
 PF00501; AMP-binding
 PF11930; DUF3448
 PF13193; DUF4009 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS