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

SERM:

CLM71_22570

SSUR:

ATE40_002195

SNEM:

NLX84_05465

SERA:

Ser39006_020655

SERQ:

CWC46_20660

PROD:

PCO85_04890

XHO:	A9255_04285

PMAG:

JI723_05680

VGA:	BSQ33_00995

VSR:	Vspart_01686(pigI)

VRU:	RND59_13750

PAG:	PLES_25871(pltF)

PAF:	PAM18_2391(pltF)

PAEL:

T223_13220

PFL:	PFL_2792(pltF)

PPRC:

PFLCHA0_c28500(tycC2)

PPRO:

PPC_2837(pltF)

PPII:

QL104_13965(pltF)

PPHE:

PP2015_465

PRR:	AT705_06620

PTU:	PTUN_a2940

PVB:	J5X90_18250

PSAZ:

PA25_35560

PSRR:

ELR70_10890

MNY:	R50073_36530

MMAI:

sS8_1539

HCH:

HCH_06032

HAHE:

ENC22_25985

HAHH:

O5O45_30020

HPRO:

LMS44_05405

MME:	Marme_4092

CARI:

FNU76_06130

CCUP:

BKK81_22625

BRH:	RBRH_03864

KIA:	G8A07_12235

PAQA:

K9V56_011395

RUG:	QC826_01035

EBA:

ebA4326

ABRE:

pbN1_28260

MOH:	IHQ72_27615

MOC:	BB934_08575

MIWA:

SS37A_37700

SIW:	GH266_23005

TSV:	DSM104635_00866(ppsD)

RPEL:

N7U68_00730

TLB:	RPE78_13960

PAED:

G5B38_20140

GEM:

GM21_0555

GEB:

GM18_3814

GUR:

Gura_2351

GBM:

Gbem_0542

GBN:	GEOBRER4_05470

GER:	KP004_01950

GSUB:

KP001_13540

GNT:	KP003_01585

GPL:	M1B72_19020

DMM:	dnm_038650

SAT:

SYN_01145

AORY:

AMOR_00680

MXA:

MXAN_4305

MSD:	MYSTI_05336 MYSTI_06018

MFB:	MFUL124B02_24105 MFUL124B02_29115

MYX:	QEG98_23025

MLAN:

JY572_36870 JY572_40520

MYM:	A176_002584

MFU:	LILAB_29675

MMAS:

MYMAC_004223

SUR:	STAUR_4842

MBD:	MEBOL_001697

CFUS:

CYFUS_005955

PBRU:

LZC95_20990 LZC95_48840

PRUE:

LVJ94_20195 LVJ94_43385 LVJ94_49200

PALJ:

LZC94_10615 LZC94_20060

SAMY:

DB32_001325

SMAM:

Mal15_54500(grsB)

PLH:	VT85_23240(tycC)

IPA:

Isop_0180

SACI:

Sinac_7429

PBOR:

BSF38_03638(dltA)

AGV:	OJF2_63240(srfAA)

TPLA:

ElP_66500(srfAC)

UHL:	UABHE_004251

AHAO:

OM944_03105

RSR:	T7867_16700

ZLA:	Q5W13_23385

WIN:

WPG_0385

EMAR:

D1013_14055

ALUT:

O5O44_10390

RLO:	GQ464_016180

NTP:	CRH09_26890

NOZ:	DMB37_03570

NOD:	FOH10_16495

NAH:	F5544_12760

SCO:	SCO5891(St3F7.11)

SHY:

SHJG_0589

SHO:	SHJGH_0422

SBH:

SBI_07708

SDV:	BN159_2476(pyr8)

SLV:	SLIV_09150

SGM:	GCM10017557_78140 GCM10017557_82750

SGRS:

V9K83_10115

STRD:

NI25_09775

SSIA:

A7J05_21360

SPUN:

BFF78_29670

SLAU:

SLA_7476

SALF:

SMD44_07462

STRO:

STRMOE7_30640

SRK:	FGW37_26810

SPAD:

DVK44_30970

SRIM:

CP984_39845

SSPB:

CP982_34450

SBRO:

GQF42_07515

SATA:

C5746_38470

SCYG:

S1361_04950(tycC1) S1361_05215(lgrB1)

SFEU:

IM697_30930

SVD:	CP969_03665

SHK:	J2N69_01105

SDD:	D9753_11310

SLF:	JEQ17_02545

SAOV:

G3H79_04215

STUB:

MMF93_27665

SCIR:

STRCI_006116

SFP:	QUY26_05335

SARM:

DVA86_03345

SCAJ:

O1G22_20925

STBR:

ABDE16_09205(redM)

STYI:

C9F11_33600(ppsB1)

ABRY:

NYE86_17005

ARUB:

J5A65_13345

NDA:

Ndas_4719

NGV:	CDO52_00495

NAKE:

KGD83_01560

AMAZ:

LUW76_14405

AMOG:

QRX60_49340

AMYZ:

HUW46_05894(pigI)

SESP:

BN6_24010

CROS:

N8J89_24230

UME:	RM788_44465

PSUU:

Psuf_005010 Psuf_018720

CATI:

CS0771_15580

DROS:

Drose_14235

PPSU:

NO713_02810(dltA)

MPRO:

BJP34_30080

NLK:	NIES25_66890

AWA:	AA650_19335

CSG:	Cylst_6224

CALO:

Cal7507_5043

BSEN:

DP114_33455

BOX:	DP113_33560

NCN:	BZZ01_10935

CALL:

OZ401_003272

KBS:	EPA93_14710

KBB:	ccbrp13_70310

» 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

All links

Gene (25)   
   MGENES (25)   
Protein sequence (136)   
   UniProt (10)   
   SWISS-PROT (4)   
   RefSeq(pep) (114)   
   PDBSTR (8)   
DNA sequence (339)   
   RefSeq(nuc) (303)   
   GenBank (22)   
   EMBL (14)   
3D Structure (3)   
   PDB (3)   
Protein domain (13)   
   InterPro (13)   
All databases (516)   

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