KEGG   ENZYME: 6.2.1.68
Entry
EC 6.2.1.68                 Enzyme                                 

Name
L-glutamate---[L-glutamyl-carrier protein] ligase;
ambE (gene name)
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
Sysname
L-glutamate:[L-glutamyl-carrier protein] ligase (AMP-forming)
Reaction(IUBMB)
ATP + L-glutamate + holo-[L-glutamyl-carrier protein] = AMP + diphosphate + L-glutamyl-[L-glutamyl-carrier protein] (overall reaction);
(1a) ATP + L-glutamate = diphosphate + (L-glutamyl)adenylate [RN:R12728];
(1b) (L-glutamyl)adenylate + holo-[L-glutamyl-carrier protein] = AMP + L-glutamyl-[L-glutamyl-carrier protein]
Reaction(KEGG)
R12728;
(other) R12729 R12730
Substrate
ATP [CPD:C00002];
L-glutamate [CPD:C00025];
holo-[L-glutamyl-carrier protein];
(L-glutamyl)adenylate [CPD:C22366]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
L-glutamyl-[L-glutamyl-carrier protein];
(L-glutamyl)adenylate [CPD:C22366]
Comment
The adenylation domain of the enzyme catalyses the activation of L-glutamate to (L-glutamyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein, or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
History
EC 6.2.1.68 created 2021
Orthology
K25234  L-glutamate---[L-glutamyl-carrier protein] ligase
Genes
PAE: PA2302(ambE)
PAEV: N297_2375
PAEI: N296_2375
PAU: PA14_34840
PAG: PLES_30021
PAF: PAM18_2738
PNC: NCGM2_3312
PAEB: NCGM1900_4228
PDK: PADK2_13760
PSG: G655_13540
PAEP: PA1S_14110
PAEM: U769_13705
PAEL: T223_15340
PAEG: AI22_19745
PAEC: M802_2372
PAEO: M801_2374
SECH: B18_23585
 » show all
Reference
1  [PMID:25814981]
  Authors
Rojas Murcia N, Lee X, Waridel P, Maspoli A, Imker HJ, Chai T, Walsh CT, Reimmann C.
  Title
The Pseudomonas aeruginosa antimetabolite L -2-amino-4-methoxy-trans-3-butenoic acid (AMB) is made from glutamate and two alanine residues via a thiotemplate-linked tripeptide precursor.
  Journal
Front Microbiol 6:170 (2015)
DOI:10.3389/fmicb.2015.00170
  Sequence
[pae:PA2302]
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.68
IUBMB Enzyme Nomenclature: 6.2.1.68
ExPASy - ENZYME nomenclature database: 6.2.1.68
BRENDA, the Enzyme Database: 6.2.1.68

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