KEGG ENZYME: 6.2.1.53

ENZYME: 6.2.1.53

Entry

EC 6.2.1.53                 Enzyme

Name

L-proline---[L-prolyl-carrier protein] ligase;
pltF (gene name);
bmp4 (gene name);
pigI (gene name)

Class

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

Sysname

L-proline:[L-prolyl-carrier protein] ligase (AMP-forming)

Reaction(IUBMB)

ATP + L-proline + holo-[L-prolyl-carrier protein] = AMP + diphosphate + L-prolyl-[L-prolyl-carrier protein] (overall reaction);
(1a) ATP + L-proline = diphosphate + (L-prolyl)adenylate [RN:R12056];
(1b) (L-prolyl)adenylate + holo-[L-prolyl-carrier protein] = AMP + L-prolyl-[L-prolyl-carrier protein]

Reaction(KEGG)

R12056;
(other) R06746 R12057

Substrate

ATP [CPD:C00002];
L-proline [CPD:C00148];
holo-[L-prolyl-carrier protein];
(L-prolyl)adenylate [CPD:C20656]

Product

AMP [CPD:C00020];
diphosphate [CPD:C00013];
L-prolyl-[L-prolyl-carrier protein];
(L-prolyl)adenylate [CPD:C20656]

Comment

The enzyme participates in the biosynthesis of several pyrrole-containing compounds, such as undecylprodigiosin, prodigiosin, pyoluteorin, and coumermycin A1. It catalyses the activation of L-proline to an adenylate form, followed by its transfer to the 4'-phosphopantheine moiety of an L-prolyl-carrier protein.

History

EC 6.2.1.53 created 2018

Pathway

ec00333

Prodigiosin biosynthesis

ec00401

Novobiocin biosynthesis

ec01100

Metabolic pathways

ec01110

Biosynthesis of secondary metabolites

Orthology

K12719

L-proline---[L-prolyl-carrier protein] ligase

K21780

L-proline---[L-prolyl-carrier protein] ligase

Genes

SMW:	SMWW4_v1c10960(pigI)

SRR:	SerAS9_1745

SRS:	SerAS12_1745

SRA:	SerAS13_1746

SERF:

L085_23070

SERA:

Ser39006_020655

SERQ:

CWC46_20660

SERM:

CLM71_22570

SSUR:

ATE40_002195

SNEM:

NLX84_05465

VGA:	BSQ33_00995

VSR:	Vspart_01686(pigI)

PRR:	AT705_06620

PTU:	PTUN_a2940

PVB:	J5X90_18250

PSAZ:

PA25_35560

LANT:

TUM19329_13350

HCH:

HCH_06032

HAHE:

ENC22_25985

HPRO:

LMS44_05405

CCUP:

BKK81_22625

CARI:

FNU76_06130

KIA:	G8A07_12235

MDR:	MDOR_11230

NTP:	CRH09_26890

NAH:	F5544_12760

SCO:	SCO5891(redM)

SLV:	SLIV_09150

SGM:	GCM10017557_78140 GCM10017557_82750

STRD:

NI25_09775

SSIA:

A7J05_21360

SALF:

SMD44_07462

SRK:	FGW37_26810

SPAD:

DVK44_30970

SRIM:

CP984_39845

SSPB:

CP982_34450

SFEU:

IM697_30930

SLF:	JEQ17_02545

SAOV:

G3H79_04215

ARUB:

J5A65_13345

NGV:	CDO52_00495

PSUU:

Psuf_018720

CATI:

CS0771_15580

» show all

Reference

1 [PMID:11880032]

Authors

Thomas MG, Burkart MD, Walsh CT.

Title

Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during undecylprodigiosin and pyoluteorin biosynthesis.

Journal

Chem Biol 9:171-84 (2002)
DOI:10.1016/S1074-5521(02)00100-X

Reference

2 [PMID:15528645]

Authors

Harris AK, Williamson NR, Slater H, Cox A, Abbasi S, Foulds I, Simonsen HT, Leeper FJ, Salmond GP

Title

The Serratia gene cluster encoding biosynthesis of the red antibiotic, prodigiosin, shows species- and strain-dependent genome context variation.

Journal

Microbiology 150:3547-60 (2004)
DOI:10.1099/mic.0.27222-0

Sequence

[ag:CAH55637]

Reference

3 [PMID:15853884]

Authors

Williamson NR, Simonsen HT, Ahmed RA, Goldet G, Slater H, Woodley L, Leeper FJ, Salmond GP

Title

Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces.

Journal

Mol Microbiol 56:971-89 (2005)
DOI:10.1111/j.1365-2958.2005.04602.x

Sequence

[ag:CAH55637]

Other DBs

ExplorEnz - The Enzyme Database:

6.2.1.53

IUBMB Enzyme Nomenclature:

6.2.1.53

ExPASy - ENZYME nomenclature database:

6.2.1.53

BRENDA, the Enzyme Database:

6.2.1.53

DBGET integrated database retrieval system