Literature summary for 6.2.1.1 extracted from

Liu, Y.; Zhu, X.; Wang, F.; Ying, T.; Li, P.; Huang, Z.; Tan, X.
Probing the role of the bridging C509 between the [Fe4S 4] cubane and the [NipNid] centre in the A-cluster of acetyl-coenzyme A synthase (2011), Chem. Commun. (Camb. ), 47, 1291-1293.

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Protein Variants

Protein Variants	Comment	Organism
C509A	site-directe mutagenesis, mutant C509A shows a significantly diminished methyl transfer activity compared to the wild-type enzyme	Moorella thermoacetica
C509H	site-directed mutagenesis, mutant C509H can accept a methyl group from CH3-Co3+FeSP at over 70% extent. The near-wild-type-level of methyl group transfer activity for C509H indicates that the di-nickel site is assembled well in this mutant, and strongly suggests that an imidazole group can bridge the di-nickel site to the cubane of the A-cluster. Histidine that replaces the bridging cysteine 509 might function as a bridge, with one nitrogen of the imidazole ring coordinating to a cubane Fe and the other nitrogen coordinating to Nip	Moorella thermoacetica
C509S	site-directed mutagenesis, mutant C509S, in which the cysteinate bridge C509 might be replaced by a serine oxide, exhibits no detectable methyl transfer activity. Oxygen is a harder donor than sulfide, and the electronic coupling between the cubane and the di-nickel site may differ relative to sulfide. Absence of methyl transfer activity in C509S indicates that an O bridge is not sufficient for this communication	Moorella thermoacetica
C509V	site-directed mutagenesis, mutant C509V exhibits no detectable methyl group transfer activity due to it lacking a bridging coordinating atom, Val is more bulky and has greater steric hindrance	Moorella thermoacetica

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	the A-cluster of acetyl-coenzyme A synthase consists of an [Fe4S4] cubane bridged to a [NipNid] centre via C509 cysteinate. The bridging cysteinate, which can be substituted by histidine imidazole, mediates communication between the [Fe4S4] cubane and the [NipNid] centre during the synthesis of acetyl-CoA	Moorella thermoacetica
Ni2+	the A-cluster of acetyl-coenzyme A synthase consists of an [Fe4S4] cubane bridged to a [NipNid] centre via C509 cysteinate. The bridging cysteinate, which can be substituted by histidine imidazole, mediates communication between the [Fe4S4] cubane and the [NipNid] centre during the synthesis of acetyl-CoA	Moorella thermoacetica

Organism

Organism	UniProt	Comment	Textmining
Moorella thermoacetica	-	-	-

Subunits

Subunits	Comment	Organism
More	the A-cluster of acetyl-coenzyme A synthase consists of an [Fe4S4] cubane bridged to a [NipNid] centre via C509 cysteinate. The bridging cysteinate, which can be substituted by histidine imidazole, mediates communication between the [Fe4S4] cubane and the [NipNid] centre during the synthesis of acetyl-CoA. The ACS/CODH from Moorella thermoacetica is an alpha2beta2 tetramer containing seven metal clusters connected by a molecular tunnel network, overview	Moorella thermoacetica

Synonyms

Synonyms	Comment	Organism
Acetyl-coenzyme A synthase	-	Moorella thermoacetica
ACS	-	Moorella thermoacetica

General Information

General Information	Comment	Organism
evolution	the metalloprotein acetyl-coenzyme A synthase/carbon monoxide dehydrogenase, ACS/CODH, is a bifunctional metalloenzyme found in anaerobic archaea and bacteria that grow hemoautotrophically on CO or CO2, and is significant for biological carbon fixation and understanding the origin of life	Moorella thermoacetica

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Release 2023.1 (January 2023)