CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018393
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
 STM4275 
Created Date
 July 27, 2013 
Organism
 Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 
NCBI Taxa ID
 99287 
Lysine Modification
Position
Peptide
Type
References
68APGNVSIKWYEDGTLacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
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 first half 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.
 REGION 411 416 Substrate binding.
 ACT_SITE 517 517
 METAL 537 537 Magnesium; via carbonyl oxygen.
 METAL 539 539 Magnesium; via carbonyl oxygen.
 METAL 542 542 Magnesium; via carbonyl oxygen.
 BINDING 311 311 Coenzyme A.
 BINDING 335 335 Coenzyme A.
 BINDING 387 387 Substrate; via amide nitrogen.
 BINDING 500 500 Substrate.
 BINDING 515 515 Substrate.
 BINDING 523 523 Coenzyme A.
 BINDING 526 526 Substrate.
 BINDING 584 584 Coenzyme A.
 MOD_RES 609 609 N6-acetyllysine.  
Keyword
 3D-structure; 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
MSQTHKHAIP ANIADRCLIN PEQYETKYKQ SINDPDTFWG EQGKILDWIT PYQKVKNTSF 60
APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DTSQSKHISY RELHRDVCRF 120
ANTLLDLGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSSS 180
RLVITADEGV RAGRSIPLKK NVDDALKNPN VTSVEHVIVL KRTGSDIDWQ EGRDLWWRDL 240
IEKASPEHQP EAMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPGDI 300
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMCQVVDKHQ VNILYTAPTA 360
IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK KIGKEKCPVV DTWWQTETGG 420
FMITPLPGAI ELKAGSATRP FFGVQPALVD NEGHPQEGAT EGNLVITDSW PGQARTLFGD 480
HERFEQTYFS TFKNMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP 540
KIAEAAVVGI PHAIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD 600
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM PS 652 
Gene Ontology
 GO:0003987; F:acetate-CoA ligase activity; IEA:HAMAP.
 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: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