KEGG   ENZYME: 6.2.1.70
Entry
EC 6.2.1.70                 Enzyme                                 
Name
L-threonine---[L-threonyl-carrier protein] ligase;
dhbF (gene name);
pmsD (gene name);
syrB1 (gene name)
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
Sysname
L-threonine:[L-threonyl-carrier protein] ligase (AMP-forming)
Reaction(IUBMB)
ATP + L-threonine + holo-[L-threonyl-carrier protein] = AMP + diphosphate + L-threonyl-[L-threonyl-carrier protein] (overall reaction);
(1a) ATP + L-threonine = diphosphate + (L-threonyl)adenylate [RN:R12772];
(1b) (L-threonyl)adenylate + holo-[L-threonyl-carrier protein] = AMP + L-threonyl-[L-threonyl-carrier protein]
Reaction(KEGG)
R12772;
(other) R12773 R12774
Substrate
ATP [CPD:C00002];
L-threonine [CPD:C00188];
holo-[L-threonyl-carrier protein];
(L-threonyl)adenylate [CPD:C22386]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
L-threonyl-[L-threonyl-carrier protein] [CPD:C21976];
(L-threonyl)adenylate [CPD:C22386]
Comment
The adenylation domain of the enzyme catalyses the activation of L-threonine to (L-threonyl)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 (as in the case of DhbF in bacillibactin biosynthesis), or of a different protein (as in the case of PmsD in pseudomonine biosynthesis). This activity is often found as part of a larger non-ribosomal peptide synthase.
History
EC 6.2.1.70 created 2021
Orthology
K16126  L-threonine---[L-threonyl-carrier protein] ligase
Genes
PPAVLOZ86_13650
PSBPsyr_2611
PSYRN018_14060
PCIPCH70_26390
PLIJKQP88_12765
PCGAXG94_03680
PMEDE3Z27_16030
PBCCD58_16125
PVKEPZ47_16295
PNBNK667_09770
PSKUKUIN1_25980
 » show all
Reference
1  [PMID:16002467]
  Authors
Vaillancourt FH, Yin J, Walsh CT
  Title
SyrB2 in syringomycin E biosynthesis is a nonheme FeII alpha-ketoglutarate- and O2-dependent halogenase.
  Journal
Proc Natl Acad Sci U S A 102:10111-6 (2005)
DOI:10.1073/pnas.0504412102
Reference
2  [PMID:18710233]
  Authors
Sattely ES, Walsh CT
  Title
A latent oxazoline electrophile for N-O-C bond formation in pseudomonine biosynthesis.
  Journal
J Am Chem Soc 130:12282-4 (2008)
DOI:10.1021/ja804499r
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.70
IUBMB Enzyme Nomenclature: 6.2.1.70
ExPASy - ENZYME nomenclature database: 6.2.1.70
BRENDA, the Enzyme Database: 6.2.1.70

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