CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007099
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
 acsA 
Gene Synonyms/Alias
 BSU29680 
Created Date
 July 27, 2013 
Organism
 Bacillus subtilis (strain 168) 
NCBI Taxa ID
 224308 
Lysine Modification
Position
Peptide
Type
References
549LPKTRSGKIMRRVLKacetylation[1]
Reference
 [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
 Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG.
 Proteomics. 2013 May;13(10-11):1726-36. [PMID: 23468065
Functional Description
 Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA 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 (By similarity). Has a role in growth and sporulation on acetate. 
Sequence Annotation
 ACT_SITE 457 457 By similarity.
 METAL 477 477 Magnesium; via carbonyl oxygen (By
 METAL 479 479 Magnesium; via carbonyl oxygen (By
 METAL 482 482 Magnesium; via carbonyl oxygen (By
 BINDING 260 260 Coenzyme A (By similarity).
 BINDING 333 333 Substrate; via amide nitrogen (By
 BINDING 440 440 Substrate (By similarity).
 BINDING 455 455 Substrate (By similarity).
 BINDING 463 463 Coenzyme A (By similarity).
 BINDING 466 466 Substrate (By similarity).
 BINDING 524 524 Coenzyme A.
 MOD_RES 549 549 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 572 AA 
Protein Sequence
MNLKALPAIE GDHNLKNYEE TYRHFDWAEA EKHFSWHETG KLNAAYEAID RHAESFRKNK 60
VALYYKDAKR DEKYTFKEMK EESNRAGNVL RRYGNVEKGD RVFIFMPRSP ELYFIMLGAI 120
KIGAIAGPLF EAFMEGAVKD RLENSEAKVV VTTPELLERI PVDKLPHLQH VFVVGGEAES 180
GTNIINYDEA AKQESTRLDI EWMDKKDGFL LHYTSGSTGT PKGVLHVHEA MIQQYQTGKW 240
VLDLKEEDIY WCTADPGWVT GTVYGIFAPW LNGATNVIVG GRFSPESWYG TIEQLGVNVW 300
YSAPTAFRML MGAGDEMAAK YDLTSLRHVL SVGEPLNPEV IRWGHKVFNK RIHDTWWMTE 360
TGSQLICNYP CMDIKPGSMG KPIPGVEAAI VDNQGNELPP YRMGNLAIKK GWPSMMHTIW 420
NNPEKYESYF MPGGWYVSGD SAYMDEEGYF WFQGRVDDVI MTSGERVGPF EVESKLVEHP 480
AIAEAGVIGK PDPVRGEIIK AFIALREGFE PSDKLKEEIR LFVKQGLAAH AAPREIEFKD 540
KLPKTRSGKI MRRVLKAWEL NLPAGDLSTM ED 572 
Gene Ontology
 GO:0003987; F:acetate-CoA ligase activity; IEA:EC.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 
Interpro
 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