CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001035
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
 acs; Rv3667; MT3768; MTV025.015 
Created Date
 July 27, 2013 
Organism
 Mycobacterium tuberculosis 
NCBI Taxa ID
 1773 
Lysine Modification
Position
Peptide
Type
References
617LPKTRSGKIMRRLLRacetylation[1]
Reference
 [1] Reversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMP.
 Xu H, Hegde SS, Blanchard JS.
 Biochemistry. 2011 Jul 5;50(26):5883-92. [PMID: 21627103
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. M.tuberculosis may use AcsA for both acetate and propionate assimilation. 
Sequence Annotation
 REGION 190 193 Coenzyme A (By similarity).
 REGION 411 416 Substrate binding (By similarity).
 ACT_SITE 525 525 By similarity.
 METAL 545 545 Magnesium; via carbonyl oxygen (By
 METAL 547 547 Magnesium; via carbonyl oxygen (By
 BINDING 311 311 Coenzyme A (By similarity).
 BINDING 387 387 Substrate; via amide nitrogen (By
 BINDING 508 508 Substrate (By similarity).
 BINDING 523 523 Substrate (By similarity).
 BINDING 531 531 Coenzyme A (By similarity).
 BINDING 534 534 Substrate (By similarity).
 MOD_RES 617 617 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
 651 AA 
Protein Sequence
MSESTPEVSS SYPPPAHFAE HANARAELYR EAEEDRLAFW AKQANRLSWT TPFTEVLDWS 60
GAPFAKWFVG GELNVAYNCV DRHVEAGHGD RVAIHWEGEP VGDRRTLTYS DLLAEVSKAA 120
NALTDLGLVA GDRVAIYLPL IPEAVIAMLA CARLGIMHSV VFGGFTAAAL QARIVDAQAK 180
LLITADGQFR RGKPSPLKAA ADEALAAIPD CSVEHVLVVR RTGIEMAWSE GRDLWWHHVV 240
GSASPAHTPE PFDSEHPLFL LYTSGTTGKP KGIMHTSGGY LTQCCYTMRT IFDVKPDSDV 300
FWCTADIGWV TGHTYGVYGP LCNGVTEVLY EGTPDTPDRH RHFQIIEKYG VTIYYTAPTL 360
IRMFMKWGRE IPDSHDLSSL RLLGSVGEPI NPEAWRWYRD VIGGGRTPLV DTWWQTETGS 420
AMISPLPGIA AAKPGSAMTP LPGISAKIVD DHGDPLPPHT EGAQHVTGYL VLDQPWPSML 480
RGIWGDPARY WHSYWSKFSD KGYYFAGDGA RIDPDGAIWV LGRIDDVMNV SGHRISTAEV 540
ESALVAHSGV AEAAVVGVTD ETTTQAICAF VVLRANYAPH DRTAEELRTE VARVISPIAR 600
PRDVHVVPEL PKTRSGKIMR RLLRDVAENR ELGDTSTLLD PTVFDAIRAA K 651 
Gene Ontology
 GO:0005618; C:cell wall; IDA:MTBBASE.
 GO:0005886; C:plasma membrane; IDA:MTBBASE.
 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:InterPro. 
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