KEGG ENZYME: 1.3.8.14

ENZYME: 1.3.8.14

Entry

EC 1.3.8.14                 Enzyme

Name

L-prolyl-[peptidyl-carrier protein] dehydrogenase;
pigA (gene name);
bmp3 (gene name);
pltE (gene name);
redW (gene name);
(L-prolyl)-[peptidyl-carrier protein]:electron-transfer flavoprotein oxidoreductase

Class

Oxidoreductases;
Acting on the CH-CH group of donors;
With a flavin as acceptor

Sysname

L-prolyl-[peptidyl-carrier protein]:electron-transfer flavoprotein oxidoreductase

Reaction(IUBMB)

L-prolyl-[peptidyl-carrier protein] + 2 electron-transfer flavoprotein = 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] + 2 reduced electron-transfer flavoprotein [RN:R06747]

Reaction(KEGG)

R06747

Substrate

L-prolyl-[peptidyl-carrier protein] [CPD:C12470];
electron-transfer flavoprotein [CPD:C04253]

Product

1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] [CPD:C12483];
reduced electron-transfer flavoprotein [CPD:C04570]

Comment

Contains FAD. The enzyme participates in the biosynthesis of several pyrrole-containing compounds, such as undecylprodigiosin, prodigiosin, pyoluteorin, and coumermycin A1. It is believed to catalyse the formation of a Delta2-pyrrolin-2-carbonyl-[peptidyl-carrier protein] intermediate, followed by a two-electron oxidation to 1H-pyrrol-2-carbonyl-[peptidyl-carrier protein].

History

EC 1.3.8.14 created 2017

Pathway

ec00333

Prodigiosin biosynthesis

ec00401

Novobiocin biosynthesis

ec01100

Metabolic pathways

ec01110

Biosynthesis of secondary metabolites

Orthology

K12721

L-prolyl-[peptidyl-carrier protein] dehydrogenase

K21782

L-prolyl-PCP dehydrogenase

Genes

SMW:	SMWW4_v1c11040(pigA)

SRR:	SerAS9_1753

SRS:	SerAS12_1753

SRA:	SerAS13_1754

SERF:

L085_23030

SERM:

CLM71_22610

SSUR:

ATE40_002235

SNEM:

NLX84_05505

PROD:

PCO85_04850

SERA:

Ser39006_020695

SERQ:

CWC46_20700

VGA:	BSQ33_17325

VSR:	Vspart_03968(pigA)

VRU:	RND59_20195

PRR:	AT705_06580

PXI:	J5O05_20760

PVB:	J5X90_18210

PSAZ:

PA25_35580

HAHH:

O5O45_30065

KIA:	G8A07_12225

PAQA:

K9V56_011385

RUG:	QC826_00990

MIWA:

SS37A_37750

NTP:	CRH09_26870

SCO:	SCO5879(redW)

SLV:	SLIV_09210

SGM:	GCM10017557_78270

STRD:

NI25_09835

SSIA:

A7J05_21380

SALF:

SMD44_07473

SRK:	FGW37_26865

SPAD:

DVK44_31035

SSPB:

CP982_34510

SFEU:

IM697_30995

SLF:	JEQ17_02480

SAOV:

G3H79_04160

STUB:

MMF93_27610

SFP:	QUY26_05280

ARUB:

J5A65_13315

AMAZ:

LUW76_14360

ACIR:

OG979_36035

» 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

Sequence

[pfl:PFL_2791] [sco:SCO5879]

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:CAH55629]

Other DBs

ExplorEnz - The Enzyme Database:

1.3.8.14

IUBMB Enzyme Nomenclature:

1.3.8.14

ExPASy - ENZYME nomenclature database:

1.3.8.14

BRENDA, the Enzyme Database:

1.3.8.14

DBGET integrated database retrieval system