| Tag | Content |
|---|
| CPLM ID | CPLM-026799 |
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 | RPA0211 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 606 | LPKTRSGKIMRRILR | acetylation | [1] |
|
Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
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 nitrogen amide (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 (By similarity).
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 | 650 AA |
Protein Sequence | MSEKIYDVPA EWASRAFVDD AKYRQMYERS VTDPTGFWAE HAKRVDWIKA PTKIDNWSFA 60
PGNVSIKWFE DGVLNAAYNC IDRHLDKRGD QVAIIWEGDD PSQSRSITYR ELHDEVCKFA 120
NILRNRNVGK GDRVTIYLPM IPEAAFAMLA CARIGAIHSV VFAGFSPDSL AGRINDCNSK 180
IVITADEGLR GGRKVPLKAN VDAALKKCEG VDWVMVVKRT GAAVEMDDVR DFWYHEAAEV 240
VTTECPVEHM HAEDPLFILY TSGSTGQPKG VLHTTGGYLV FASMTHQYVF DYHDGDIYWC 300
TADVGWVTGH SYILYGPLAN GATTLMFEGV PNYPTNSRFW EVIDKHKVNI FYTAPTAIRA 360
LMQAGDEPVK KTSRKSLRLL GSVGEPINPE AWEWYHRVVG EDRCPIVDTW WQTETGGILI 420
TPLPGATKLK PGSATRPFFG VVPEILDPEG NVLEGECTGN LCLARSWPGQ MRTVYGDHAR 480
FEQTYFSAYK GKYFTGDGCR RDTDGFYWIT GRVDDVINVS GHRMGTAEVE SSLVAHPKVS 540
EAAVVGYPHD IKGQGIYAYV TLMAGEEPTE ELRKELVAWV RKDIGPIASP DLIQFAPGLP 600
KTRSGKIMRR ILRKIAEDEP SSLGDTSTLA DPAVVDDLVE HRQNKHHKAS 650 |
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 | |