KEGG ENZYME: 6.2.1.67

ENZYME: 6.2.1.67

Entry

EC 6.2.1.67                 Enzyme

Name

L-alanine---[L-alanyl-carrier protein] ligase;
ambB (gene name);
phsB (gene name)

Class

Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases

Sysname

L-alanine:[L-alanyl-carrier protein] ligase (AMP-forming)

Reaction(IUBMB)

ATP + L-alanine + holo-[L-alanyl-carrier protein] = AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein] (overall reaction);
(1a) ATP + L-alanine = diphosphate + (L-alanyl)adenylate [RN:R12725];
(1b) (L-alanyl)adenylate + holo-[L-alanyl-carrier protein] = AMP + L-alanyl-[L-alanyl-carrier protein]

Reaction(KEGG)

R12725;
(other) R12726 R12727

Substrate

ATP [CPD:C00002];
L-alanine [CPD:C00041];
holo-[L-alanyl-carrier protein];
(L-alanyl)adenylate [CPD:C22363]

Product

AMP [CPD:C00020];
diphosphate [CPD:C00013];
L-alanyl-[L-alanyl-carrier protein];
(L-alanyl)adenylate [CPD:C22363]

Comment

The adenylation domain of the enzyme catalyses the activation of L-alanine to (L-alanyl)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 6.2.1.67 created 2021

Orthology

K12912

phosphinothricin tripeptide synthetase phsB

K25233

L-alanine---[L-alanyl-carrier protein] ligase

Genes

PAE:	PA2305(ambB)

PAEV:

N297_2378(lgrD)

PAEI:

N296_2378(lgrD)

PAU:	PA14_34810(mxaA)

PAG:	PLES_29991

PAF:	PAM18_2735

PNC:	NCGM2_3315(mxaA)

PAEB:

NCGM1900_4225

PDK:	PADK2_13745

PSG:	G655_13525

PAEP:

PA1S_14095

PAER:

PA1R_gp0106

PAEM:

U769_13690

PAEL:

T223_15325

PAES:

SCV20265_3018

PAEU:

BN889_02519

PAEG:

AI22_19760

PAEC:

M802_2375

PAEO:

M801_2377

SECH:

B18_23600

MHAW:

RMN56_02105

» show all

Reference

1 [PMID:16251301]

Authors

Schwartz D, Grammel N, Heinzelmann E, Keller U, Wohlleben W.

Title

Phosphinothricin tripeptide synthetases in Streptomyces viridochromogenes Tu494.

Journal

Antimicrob Agents Chemother 49:4598-607 (2005)
DOI:10.1128/AAC.49.11.4598-4607.2005

Sequence

[ag:CAJ14037]

Reference

2 [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:PA2305]

Other DBs

ExplorEnz - The Enzyme Database:

6.2.1.67

IUBMB Enzyme Nomenclature:

6.2.1.67

ExPASy - ENZYME nomenclature database:

6.2.1.67

BRENDA, the Enzyme Database:

6.2.1.67

DBGET integrated database retrieval system