| Tag | Content |
|---|
| CPLM ID | CPLM-011554 |
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 | RPE_0069 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain BisA53) |
NCBI Taxa ID | 316055 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 606 | LPKTRSGKIMRRILR | acetylation | [1] |
|
Reference | [1] Reversible N epsilon-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris. Crosby HA, Heiniger EK, Harwood CS, Escalante-Semerena JC. Mol Microbiol. 2010 May;76(4):874-88. [ PMID: 20345662] |
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). |
Sequence Annotation | REGION 408 413 Substrate binding (By similarity).
ACT_SITE 514 514 By similarity.
METAL 534 534 Magnesium; via carbonyl oxygen (By
METAL 536 536 Magnesium; via carbonyl oxygen (By
METAL 539 539 Magnesium; via carbonyl oxygen (By
BINDING 308 308 Coenzyme A (By similarity).
BINDING 332 332 Coenzyme A (By similarity).
BINDING 384 384 Substrate; via amide nitrogen (By
BINDING 497 497 Substrate (By similarity).
BINDING 512 512 Substrate (By similarity).
BINDING 520 520 Coenzyme A (By similarity).
BINDING 523 523 Substrate (By similarity).
BINDING 581 581 Coenzyme A.
MOD_RES 606 606 N6-acetyllysine (By similarity). |
Keyword | Acetylation; ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding; Nucleotide-binding. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 648 AA |
Protein Sequence | MSEKIYDVPA EWAKRAFVDD AKYQEMYARS VNDPNGFWKD EAQRVDWIKP FSVVENTSFA 60
PGNVSIKWFE DGVLNVAANC IDRHLKDRAD QVAIIWEGDD PSESRKITYR QLHDEVCKMA 120
NVLRNRNVQK GDRVTIYLPM IPEAAFAMLA CARIGAIHSV VFGGFSPDSL AQRITDCASK 180
VVITADEGLR GGRTVPLKAN VDAALRKSSA VDWVVVVKRT GADVFMDDVR DFWYHEAAEM 240
VTTECPVEPM HAEDPLFILY TSGSTGQPKG VLHTTGGYLV FASMTHQYVF DYHDGDVYWC 300
TADVGWVTGH SYILYGPLAN GATTLMFEGV PNYPTNSRFW EVIDKHQVNI FYTAPTAIRA 360
LMQGGDEPVT KTSRKSLRLL GSVGEPINPE AWEWYHRVVG EDRCPIVDTW WQTETGGILI 420
TPLPGATKLK PGSATRPFFG VVPQIMDADA NVLEGECTGN LCLAKSWPGQ MRTVYGDHAR 480
FEQTYFSAYP GKYFTGDGCR RDADGYYWIT GRVDDVINVS GHRMGTAEVE SSLVAHPQVS 540
EAAVVGYPHD IKGQGIYAYV TLMTGVEPTE ALRKELVAWV RKDIGPIASP DLIQFAPGLP 600
KTRSGKIMRR ILRKIAEDES STLGDTSTLA DPGVVSELVE HRQNKRHV 648 |
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:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |