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CAZyme Information: MGYG000003372_00928
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Citrobacter werkmanii | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter werkmanii | |||||||||||
| CAZyme ID | MGYG000003372_00928 | |||||||||||
| CAZy Family | GT2 | |||||||||||
| CAZyme Description | Acetyl-coenzyme A synthetase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 26166; End: 28124 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd05967 | PrpE | 0.0 | 24 | 638 | 1 | 614 | Propionyl-CoA synthetase (PrpE). EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency. |
| TIGR02188 | Ac_CoA_lig_AcsA | 0.0 | 18 | 644 | 1 | 626 | acetate--CoA ligase. This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501. |
| cd05966 | ACS | 0.0 | 22 | 634 | 1 | 608 | Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme). Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation. |
| cd17634 | ACS-like | 0.0 | 24 | 611 | 1 | 587 | acetate-CoA ligase. This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain. |
| cd05968 | AACS_like | 0.0 | 22 | 635 | 7 | 610 | Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase. This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CAE6201330.1 | 1.66e-248 | 20 | 642 | 578 | 1210 |
| CAE6201338.1 | 2.28e-248 | 20 | 642 | 589 | 1221 |
| QND46664.1 | 8.12e-24 | 91 | 615 | 2088 | 2576 |
| BAY30132.1 | 8.18e-24 | 60 | 615 | 566 | 1079 |
| BAY90071.1 | 1.43e-23 | 81 | 622 | 579 | 1089 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2P2Q_A | 0.0 | 1 | 652 | 1 | 652 | ChainA, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium],2P2Q_B Chain B, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium] |
| 2P2J_A | 0.0 | 1 | 652 | 1 | 652 | ChainA, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium],2P2J_B Chain B, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium] |
| 2P2M_A | 0.0 | 1 | 652 | 1 | 652 | ChainA, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium],2P2M_B Chain B, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium] |
| 2P2F_A | 0.0 | 1 | 652 | 1 | 652 | ChainA, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium],2P2F_B Chain B, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium] |
| 5JRH_A | 0.0 | 1 | 652 | 1 | 652 | Crystalstructure of Salmonella enterica acetyl-CoA synthetase (Acs) in complex with cAMP and Coenzyme A [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],5JRH_B Crystal structure of Salmonella enterica acetyl-CoA synthetase (Acs) in complex with cAMP and Coenzyme A [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q7MBA6 | 0.0 | 1 | 650 | 1 | 650 | Acetyl-coenzyme A synthetase OS=Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) OX=243265 GN=acs PE=3 SV=1 |
| Q8D1G8 | 0.0 | 1 | 652 | 1 | 652 | Acetyl-coenzyme A synthetase OS=Yersinia pestis OX=632 GN=acs PE=3 SV=2 |
| Q87KU7 | 0.0 | 1 | 645 | 1 | 646 | Acetyl-coenzyme A synthetase OS=Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) OX=223926 GN=acsA PE=3 SV=1 |
| Q7MGU3 | 0.0 | 1 | 645 | 1 | 646 | Acetyl-coenzyme A synthetase OS=Vibrio vulnificus (strain YJ016) OX=196600 GN=acsA PE=3 SV=2 |
| Q8DCZ9 | 0.0 | 1 | 645 | 1 | 646 | Acetyl-coenzyme A synthetase OS=Vibrio vulnificus (strain CMCP6) OX=216895 GN=acsA PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.999866 | 0.000177 | 0.000004 | 0.000000 | 0.000000 | 0.000000 |