KEGG   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
IZH: FEM41_11915
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
SERA: Ser39006_020695
SERQ: CWC46_20700
PROD: PCO85_04850
XHO: A9255_04280
PMAG: JI723_05675
VGA: BSQ33_17325
VSR: Vspart_03968(pigA)
VRU: RND59_20195
PAG: PLES_25861(pltE)
PAF: PAM18_2390(pltE)
PAEL: T223_13215
PFL: PFL_2791(pltE)
PPRC: PFLCHA0_c28490(mmgC4)
PPRO: PPC_2836(pltE)
PPII: QL104_13960(pltE)
PPHE: PP2015_464
PRR: AT705_06580
PTU: PTUN_a2937
PXI: J5O05_20760
PVB: J5X90_18210
PSAZ: PA25_35580
MMAI: sS8_1540
HCH: HCH_06021
HAHE: ENC22_25940
HAHH: O5O45_30065
HPRO: LMS44_05385
MME: Marme_4091
CARI: FNU76_06120
CCUP: BKK81_22635
BRH: RBRH_01923 RBRH_03863
KIA: G8A07_12225
PAQA: K9V56_011385
RUG: QC826_00990
EBA: ebA4327
ABRE: pbN1_28250(acdA2)
MOH: IHQ72_27610
MOC: BB934_08570
MIWA: SS37A_37750
SIW: GH266_22965
TSV: DSM104635_00867(acdA_5)
RPEL: N7U68_00740
PAED: G5B38_20150
ACRO: K3J57_15270
GEM: GM21_0556
GEB: GM18_3813
GUR: Gura_2352
GBM: Gbem_0543
GBN: GEOBRER4_05480
GER: KP004_01955
GSUB: KP001_13535
GNT: KP003_01590
GPL: M1B72_19015
PEF: A7E78_03240
DES: DSOUD_2098
DMM: dnm_038660
SAT: SYN_01146
AORY: AMOR_00670
MXA: MXAN_4304
MSD: MYSTI_05335 MYSTI_06017
MYM: A176_002585
MFB: MFUL124B02_24100
MYX: QEG98_23020
MLAN: JY572_36875 JY572_40525
MFU: LILAB_29670
MMAS: MYMAC_004222
SUR: STAUR_4841
MBD: MEBOL_001696 MEBOL_007008
CFUS: CYFUS_005954
SAMY: DB32_001324
LGY: T479_05845
PAEQ: R50912_17985
PLUT: EI981_06705
ESS: ATZ33_00115
CCB: Clocel_2633
CSR: Cspa_c03050(acdA)
CRW: CROST_036530(acdA) CROST_042510(pigA)
CFB: CLFE_005400(pigA) CLFE_011230(acdA)
CAUN: CLAUR_012590(acdA) CLAUR_032520(pigA)
VGU: HYG85_05660
VPY: HZI73_06095
SEDZ: JYG23_13425
NTP: CRH09_26870
NOZ: DMB37_03565
NOD: FOH10_16490
NAH: F5544_12765
SCO: SCO5879(redW)
SGB: WQO_24555 WQO_29010
SANL: KZO11_19765
SHY: SHJG_0588
SHO: SHJGH_0421
SBH: SBI_07709(fadE30)
SDV: BN159_2475(pyr7)
SLV: SLIV_09210
SPRI: SPRI_0152 SPRI_0225 SPRI_7128 SPRI_7201
SCZ: ABE83_19775
SGM: GCM10017557_78270 GCM10017557_82740
STRD: NI25_09835
SSIA: A7J05_21380
SVU: B1H20_15480
SPUN: BFF78_29675
SLAU: SLA_2867 SLA_7475
SALF: SMD44_07473
STRO: STRMOE7_30645
SRJ: SRO_6332
SQZ: FQU76_00515 FQU76_33225
SGZ: C0216_31280
SRK: FGW37_26865
SPAD: DVK44_31035
SAQU: EJC51_24885
SGF: HEP81_06681
SCAV: CVT27_14810
SSUB: CP968_00515
STSU: B7R87_00410
SSPB: CP982_34510
SBRO: GQF42_07510
SATA: C5746_38465
SCYG: S1361_04960(acdA1)
SFEU: IM697_30995
SLIA: HA039_01155
SVD: CP969_03660
SCAL: I6J39_15495
SXN: IAG42_36785
SHK: J2N69_01110
STRY: EQG64_15535
SDD: D9753_08585 D9753_11315 D9753_34405
SLF: JEQ17_02480
SAOV: G3H79_04160
STUB: MMF93_27610
SCIR: STRCI_006117
SDRZ: NEH16_32305
SCOA: QU709_09960
SROC: RGF97_13740
SFP: QUY26_05280
SARM: DVA86_03340 DVA86_18290
SCAJ: O1G22_20930
ABRY: NYE86_17000
ARUB: J5A65_13315
NDA: Ndas_4720
NAL: B005_4297
NGV: CDO52_00490
NAKE: KGD83_01555
STRR: EKD16_15785(mmgC6)
AMAZ: LUW76_14360
ACIR: OG979_36035
NGN: LCN96_24155
MHAI: OHB01_08835
AMYB: BKN51_28030
AMOG: QRX60_49345
SESP: BN6_24020
KPHY: AOZ06_22105 AOZ06_42060
LED: BBK82_35560
ALO: CRK58154 CRK58857 CRK62141
CROS: N8J89_24220
UME: RM788_51330
MFEU: H1D33_25750
ACTR: Asp14428_17360
AOU: ACTOB_006435
PSUU: Psuf_018910
CATI: CS0771_15590
DROS: Drose_14255
NHY: JQS43_11190
PPSU: NO713_02809(pltE)
MPRO: BJP34_30085
AWA: AA650_19340
CSG: Cylst_6223
CALO: Cal7507_5042
BSEN: DP114_33460
BOX: DP113_33565
NCN: BZZ01_10930
KBS: EPA93_14715
KBB: ccbrp13_70320
SMAM: Mal15_54510(acdA)
PLH: VT85_13010(acdA)
IPA: Isop_1449
SACI: Sinac_1586
PBOR: BSF38_05639(acdA)
AGV: OJF2_60380(acdA_2)
TPLA: ElP_61390(acdA)
RSR: T7867_16695
WIN: WPG_0386
ALUT: O5O44_10395
RLO: GQ464_016185
 » 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
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