| Tag | Content |
|---|
| CPLM ID | CPLM-013883 |
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 | TTHA1248 |
Created Date | July 27, 2013 |
Organism | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
NCBI Taxa ID | 300852 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 9 | DRLESVLKEERVFYP | acetylation | [1] | | 72 | EGDLPHPKWFVGGKT | acetylation | [1] |
|
Reference | [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus. Okanishi H, Kim K, Masui R, Kuramitsu S. J Proteome Res. 2013 Aug 1;. [ PMID: 23901841] |
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 413 418 Substrate binding (By similarity).
ACT_SITE 520 520 By similarity.
METAL 540 540 Magnesium; via carbonyl oxygen (By
METAL 542 542 Magnesium; via carbonyl oxygen (By
METAL 545 545 Magnesium; via carbonyl oxygen (By
BINDING 313 313 Coenzyme A (By similarity).
BINDING 337 337 Coenzyme A (By similarity).
BINDING 389 389 Substrate; via amide nitrogen (By
BINDING 503 503 Substrate (By similarity).
BINDING 518 518 Substrate (By similarity).
BINDING 529 529 Substrate (By similarity).
BINDING 587 587 Coenzyme A.
MOD_RES 612 612 N6-acetyllysine (By similarity). |
Keyword | Acetylation; ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 648 AA |
Protein Sequence | MDRLESVLKE ERVFYPSEEF RKQAHIKSEE EYQRLYEESV RDPEGFWGRV ASELHWFEPW 60
RKVLEGDLPH PKWFVGGKTN LSYNALDRHV KTWRRNKAAI VWEGEPGEER VLTYHDLWRE 120
VQRFANVLKR LGVKKGDRVT IYLPMIPEAA IAMLACTRIG AVHSVVFGGF SAGALADRIK 180
DAEAKVLITA DGGFRRGGIV PLKQNADEAL KDATSVEHVV VVRRTGEEVP WTPGRDHWWH 240
ELMEAAPDRC DPEPMEAEEP LFILYTSGST GKPKGVLHTT GGYMTYVYYT TKLVFDLKDE 300
DVYWCTADVG WITGHSYVVY GPLLNGATTV MYEGAPNWPE PDRFWRIVDK YGVTVFYTAP 360
TAIRSFMKWG EGWPGKHRLD SLRLLGTVGE PINPEAWLWY YHVIGKGRCP IVDTWWQTET 420
GGIMITTLPG AHAMKPGHAG KPFFGVVPEI LDGEHRPVEN PDEGGHLCIT RPWPSMLRTV 480
WGDPERFLQQ YFSQHPGVYF SGDGAKRDKD GYYMILGRVD DVLNVAGHRL GTMEIESALV 540
AHPAVAEAAV VGRPDPVKGE AIVAFVTLKE GHTPSDALKE ELRAHVAKVI GPIARPDEIR 600
FTDALPKTRS GKIMRRLLRQ IAAGEKEIKG DTSTLEDRSV VERLKEGA 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 | |