KEGG   ENZYME: 6.2.1.69
Entry
EC 6.2.1.69                 Enzyme                                 

Name
L-cysteine---[L-cysteinyl-carrier protein] ligase;
pchE (gene name);
pchF (gene name);
angR (gene name)
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
Sysname
L-cysteine:[L-cysteinyl-carrier protein] ligase (AMP-forming)
Reaction(IUBMB)
ATP + L-cysteine + holo-[L-cysteinyl-carrier protein] = AMP + diphosphate + L-cysteinyl-[L-cysteinyl-carrier protein] (overall reaction);
(1a) ATP + L-cysteine = diphosphate + (L-cysteinyl)adenylate [RN:R12765];
(1b) (L-cysteinyl)adenylate + holo-[L-cysteinyl-carrier protein] = AMP + L-cysteinyl-[L-cysteinyl-carrier protein]
Reaction(KEGG)
R12765;
(other) R12766 R12767
Substrate
ATP [CPD:C00002];
L-cysteine [CPD:C00097];
holo-[L-cysteinyl-carrier protein];
(L-cysteinyl)adenylate [CPD:C22385]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
L-cysteinyl-[L-cysteinyl-carrier protein];
(L-cysteinyl)adenylate [CPD:C22385]
Comment
The adenylation domain of the enzyme catalyses the activation of L-cysteine to (L-cysteinyl)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 6.2.1.69 created 2021
Pathway
ec01053  Biosynthesis of siderophore group nonribosomal peptides
Orthology
K12239  L-cysteine---[L-cysteinyl-carrier protein] ligase PchE
K12240  L-cysteine---[L-cysteinyl-carrier protein] ligase PchF
Genes
KMI: VW41_14180
PGE: LG71_13430 LG71_26195
SYM: K6K13_09575
YPE: YPO0776
YPA: YPA_3374
YPN: YPN_3216
YPM: YP_3425(entF3)
YPZ: YPZ3_0722
YPT: A1122_01155
YPD: YPD4_0678
YPX: YPD8_0678
YPW: CH59_1087
YPJ: CH55_3520
YPV: BZ15_2798
YPL: CH46_140
YPS: YPTB3296
YPO: BZ17_3313
YPY: YPK_0752
YPB: YPTS_3434
YPQ: DJ40_3145
YPU: BZ21_2577
YPR: BZ20_2822
YPC: BZ23_2860
YPF: BZ19_2700
YFR: AW19_774
YKR: CH54_888
XBV: XBW1_1484
PAE: PA4225(pchF) PA4226(pchE)
PAU: PA14_09270(pchE) PA14_09280(pchF) PA14_54920
PAP: PSPA7_0874(pchE) PSPA7_0875(pchF)
PAG: PLES_07011(pchE) PLES_07021(pchF)
PAF: PAM18_0711(pchE) PAM18_0712(pchF)
PNC: NCGM2_5470(pchF) NCGM2_5471(pchE)
PAEB: NCGM1900_0733(pchE) NCGM1900_0734(pchF)
PAEU: BN889_04699(pchF) BN889_04700(pchE_1) BN889_04701(pchE_2)
PFL: PFL_3492(pchF) PFL_3493(pchE)
PPRC: PFLCHA0_c35330(irp1) PFLCHA0_c35340(irp2)
PPRO: PPC_3646(pchF) PPC_3647(pchE)
PFB: VO64_5522
PSOS: POS17_3635(pchF) POS17_3636(pchE)
PSEN: PNC201_20480(mbtB)
MEC: Q7C_386
ADI: B5T_02512
RSO: RSc1811
RSE: F504_1578
BPS: BPSS0586(pchE) BPSS0587(pchF)
BPZ: BP1026B_II0646(pchE) BP1026B_II0647(pchF)
BCJ: BCAM2230(pchE)
BCEO: I35_6120(pchF) I35_6121(pchE)
BGP: BGL_1c20570(pchF) BGL_1c20580(pchE)
RPC: RPC_3032
ALI: AZOLI_p20160(pchE) AZOLI_p20161(pchF)
SANC: SANR_1291
CKL: CKL_1511
CKR: CKR_1405
CSB: CLSA_c16940(irp2)
BPRO: PMF13cell1_00657(mbtB_1)
EHL: EHLA_1441
DSY: DSY2821
DHD: Dhaf_3965
DAE: Dtox_2674
MANA: MAMMFC1_02828(mbtB_2)
STED: SPTER_12030(mbtB_1)
MPA: MAP_3742
MAVI: RC58_00135
MAVU: RE97_00135
CDH: CDB402_1084(irp2C)
CDZ: CD31A_2083(irp2C)
CDS: CDC7B_2042(irp2C)
CDD: CDCE8392_1964(irp2C)
CDIP: ERS451417_02094(irp2C)
CSX: CSING_01210(irp2C)
CSP: WM42_1816
NFR: ERS450000_00763(mbtB_1)
SCO: SCO7683(SC4C2.18)
SGU: SGLAU_04465(nrps1B) SGLAU_04470(nrps1C) SGLAU_04640(nrps1D) SGLAU_04650(nrps1E)
STRE: GZL_p00202
STRD: NI25_03970
SHUN: DWB77_06824(mbtB_1)
CMI: CMM_0330(npsB)
CMC: CMN_00301(npsB)
DCO: SAMEA4475696_1592(mbtB_3)
PAUS: NCTC13651_00740(mbtB_1)
SRO: Sros_3767
SACC: EYD13_12025(mbtB1)
PAUT: Pdca_37550
ASE: ACPL_6139(nrps2A) ACPL_6158(nrps2C)
EYY: EGYY_00410(EntF)
AEQ: AEQU_0074
 » show all
Reference
1  [PMID:10555976]
  Authors
Quadri LE, Keating TA, Patel HM, Walsh CT
  Title
Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE, and PchF.
  Journal
Biochemistry 38:14941-54 (1999)
DOI:10.1021/bi991787c
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.69
IUBMB Enzyme Nomenclature: 6.2.1.69
ExPASy - ENZYME nomenclature database: 6.2.1.69
BRENDA, the Enzyme Database: 6.2.1.69

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