KEGG   ENZYME: 6.2.1.56Help
Entry
EC 6.2.1.56                 Enzyme                                 

Name
4-hydroxybutyrate---CoA ligase (ADP-forming);
Nmar_0206 (locus name)
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
BRITE hierarchy
Sysname
4-hydroxybutanoate:CoA ligase (ADP-forming)
Reaction(IUBMB)
ATP + 4-hydroxybutanoate + CoA = ADP + phosphate + 4-hydroxybutanoyl-CoA [RN:R10758]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
4-hydroxybutanoate [CPD:C00989];
CoA [CPD:C00010]
Product
ADP [CPD:C00008];
phosphate [CPD:C00009];
4-hydroxybutanoyl-CoA [CPD:C11062]
Comment
The enzyme, characterized from the marine ammonia-oxidizing archaeon Nitrosopumilus maritimus, participates in a variant of the 3-hydroxypropanoate/4-hydroxybutanate CO2 fixation cycle. cf. EC 6.2.1.40, 4-hydroxybutyrate---CoA ligase (AMP-forming).
History
EC 6.2.1.56 created 2019
Pathway
ec00720  Carbon fixation pathways in prokaryotes
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K18593  4-hydroxybutyrate---CoA ligase (ADP-forming)
Genes
NMR: Nmar_0206
NIR: NSED_00830
NID: NPIRD3C_0595
NIN: NADRNF5_2051
NCT: NMSP_1506(sucD_2)
CSY: CENSYa_0021
NGA: Ngar_c26620
NVN: NVIE_024650
NEV: NTE_01051
TAA: NMY3_00758(sucD_1)
NBV: T478_1249
NDV: NDEV_0180(hbcS)
 » show all
Taxonomy
Reference
1  [PMID:24843170]
  Authors
Konneke M, Schubert DM, Brown PC, Hugler M, Standfest S, Schwander T, Schada von Borzyskowski L, Erb TJ, Stahl DA, Berg IA.
  Title
Ammonia-oxidizing archaea use the most energy-efficient aerobic pathway for CO2 fixation.
  Journal
Proc Natl Acad Sci U S A 111:8239-44 (2014)
DOI:10.1073/pnas.1402028111
  Sequence
[nmr:Nmar_0206]
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.56
IUBMB Enzyme Nomenclature: 6.2.1.56
ExPASy - ENZYME nomenclature database: 6.2.1.56
BRENDA, the Enzyme Database: 6.2.1.56

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