logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002341_01971

You are here: Home > Sequence: MGYG000002341_01971

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 Acinetobacter ursingii
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter; Acinetobacter ursingii
CAZyme ID MGYG000002341_01971
CAZy Family GT2
CAZyme Description Acetyl-coenzyme A synthetase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
647 MGYG000002341_9|CGC2 72295.97 5.4895
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002341 3456217 Isolate United States North America
Gene Location Start: 116679;  End: 118622  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002341_01971.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd05968 AACS_like 0.0 21 633 8 610
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.
PRK10524 prpE 0.0 21 637 3 621
propionyl-CoA synthetase; Provisional
cd17634 ACS-like 0.0 22 609 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.
COG0365 Acs 0.0 66 622 1 525
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism].
cd05967 PrpE 0.0 22 639 1 617
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CAE6201330.1 1.39e-245 4 641 564 1211
CAE6201338.1 1.90e-245 4 641 575 1222
AFZ04852.1 8.20e-20 65 613 571 1074
CAE6256584.1 1.06e-17 251 616 1706 2058
AFY93865.1 8.61e-16 77 613 330 842

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2P2F_A 5.67e-319 22 640 24 642
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 8.41e-319 22 640 24 642
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]
2P2M_A 1.70e-318 22 640 24 642
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]
2P2B_A 2.55e-318 22 640 24 642
ChainA, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium],2P2B_B Chain B, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium]
2P2Q_A 3.40e-318 22 640 24 642
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q4UP35 0.0 1 640 1 641
Acetyl-coenzyme A synthetase OS=Xanthomonas campestris pv. campestris (strain 8004) OX=314565 GN=acsA PE=3 SV=1
Q885K7 0.0 4 642 6 644
Acetyl-coenzyme A synthetase OS=Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000) OX=223283 GN=acsA PE=3 SV=1
Q7MGU3 0.0 4 641 6 644
Acetyl-coenzyme A synthetase OS=Vibrio vulnificus (strain YJ016) OX=196600 GN=acsA PE=3 SV=2
Q6LLZ1 0.0 4 641 6 643
Acetyl-coenzyme A synthetase OS=Photobacterium profundum (strain SS9) OX=298386 GN=acsA PE=3 SV=1
Q88EH6 0.0 4 642 6 644
Acetyl-coenzyme A synthetase 1 OS=Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) OX=160488 GN=acsA1 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
1.000064 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002341_01971.