Tag | Content |
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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 |
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68 | APGNVSIKWYEDGTL | acetylation | [1] |
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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 |
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