KEGG   ENZYME: 6.2.1.66
Entry
EC 6.2.1.66                 Enzyme                                 

Name
glyine---[glycyl-carrier protein] ligase;
dhbF (gene name);
sfmB (gene name)
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
Sysname
glycine:[glycyl-carrier protein] ligase (AMP-forming)
Reaction(IUBMB)
ATP + glycine + holo-[glycyl-carrier protein] = AMP + diphosphate + glycyl-[glycyl-carrier protein] (overall reaction);
(1a) ATP + glycine = diphosphate + (glycyl)adenylate [RN:R12721];
(1b) (glycyl)adenylate + holo-[glycyl-carrier protein] = AMP + glycyl-[glycyl-carrier protein]
Reaction(KEGG)
R12721;
(other) R12722 R12723
Substrate
ATP [CPD:C00002];
glycine [CPD:C00037];
holo-[glycyl-carrier protein];
(glycyl)adenylate [CPD:C22361]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
glycyl-[glycyl-carrier protein];
(glycyl)adenylate [CPD:C22361]
Comment
The adenylation domain of the enzyme catalyses the activation of glycine to (glycyl)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 (as in the case of DhbF in bacillibactin biosynthesis), or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
History
EC 6.2.1.66 created 2021
Pathway
ec01053  Biosynthesis of siderophore group nonribosomal peptides
Orthology
K04780  glyine---[glycyl-carrier protein] ligase
Genes
BRH: RBRH_00578
VPE: Varpa_4519
VPD: VAPA_1c40300
JAG: GJA_3056(dhbF)
BSU: BSU31960(dhbF)
BSR: I33_3287
BSL: A7A1_2308
BSH: BSU6051_31960(dhbF)
BSY: I653_15395
BSUT: BSUB_03414(dhbF)
BSUL: BSUA_03414(dhbF)
BSUS: Q433_17480(dhbF)
BSO: BSNT_09659(dhbF)
BSQ: B657_31960(dhbF)
BSX: C663_3055
BSS: BSUW23_15540(dhbF)
BST: GYO_3487
BLI: BL04024(dhbF)
BLD: BLi03898(dhbF)
BLH: BaLi_c39150(dhbF)
BAQ: BACAU_2929(dhbF)
BYA: BANAU_3090(dhbF)
BAMP: B938_14845(dhbF)
BAML: BAM5036_2817(dhbF)
BAMA: RBAU_3032(dhbF)
BAMN: BASU_2823(dhbF)
BAMB: BAPNAU_3080(dhbF)
BAMT: AJ82_16420
BAMY: V529_31610(dhbF)
BMP: NG74_03051(dhbF)
BAO: BAMF_2992(dhbF)
BAZ: BAMTA208_15880(dhbF)
BQL: LL3_03265(dhbF)
BXH: BAXH7_03248(dhbF)
BQY: MUS_3488(dhbF)
BAMI: KSO_004640
BAMC: U471_30070
BAMF: U722_15635
BSON: S101395_00491(entF)
BMOJ: HC660_30810(dhbF)
BAN: BA_2372(dhbF)
BAR: GBAA_2372(dhbF)
BAT: BAS2208
BAH: BAMEG_2228(bacF)
BAI: BAA_2430(bacF)
BANT: A16_24050
BANR: A16R_24320
BANV: DJ46_1161(dltA)
BCA: BCE_2402(dhbF)
BCZ: BCE33L2131(entF)
BCR: BCAH187_A2472(bacF)
BCB: BCB4264_A2337(bacF)
BCU: BCAH820_2390(bacF)
BCG: BCG9842_B2988(bacF)
BCQ: BCQ_2298(dhbF)
BCX: BCA_2439(bacF)
BAL: BACI_c23170(rimI5)
BNC: BCN_2293
BCF: bcf_11800
BCER: BCK_23055
BTK: BT9727_2147(entF)
BTL: BALH_2111(entF)
BTB: BMB171_C2077(bacF)
BTT: HD73_2593
BTC: CT43_CH2269(bacF)
BTM: MC28_1578
BTG: BTB_c23880(dhbF)
BTI: BTG_08300
BTW: BF38_3557(dltA)
BWW: bwei_2663(dltA3)
BMYO: BG05_3688(dltA)
BMYC: DJ92_4947(dltA)
BPUS: UP12_18995
BJS: MY9_3208
BACW: QR42_18505
BACP: SB24_14220
BACB: OY17_17830
BACY: QF06_14305
BACL: BS34A_34930(dhbF)
BALM: BsLM_3191
BGY: BGLY_4305(dhbF)
BEO: BEH_16975
OIH: OB0958(dhbF)
ANM: GFC28_2443(dltA)
ANL: GFC29_2992(dltA)
PLV: ERIC2_c15760(dhbF)
SIV: SSIL_0953
PFT: JBW_01674
MSHO: MSHO_41470
CPRE: Csp1_26920(dhbF_2)
ROP: ROP_20370
TPR: Tpau_3693
SGR: SGR_6739
SGB: WQO_01320
SFI: SFUL_387
SALJ: SMD11_0929(dhbF)
SFK: KY5_3423
 » show all
Reference
1  [PMID:11112781]
  Authors
May JJ, Wendrich TM, Marahiel MA
  Title
The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin.
  Journal
J Biol Chem 276:7209-17 (2001)
DOI:10.1074/jbc.M009140200
  Sequence
[bsu:BSU31960]
Reference
2  [PMID:17981978]
  Authors
Li L, Deng W, Song J, Ding W, Zhao QF, Peng C, Song WW, Tang GL, Liu W
  Title
Characterization of the saframycin A gene cluster from Streptomyces lavendulae NRRL 11002 revealing a nonribosomal peptide synthetase system for assembling the unusual tetrapeptidyl skeleton in an iterative manner.
  Journal
J Bacteriol 190:251-63 (2008)
DOI:10.1128/JB.00826-07
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.66
IUBMB Enzyme Nomenclature: 6.2.1.66
ExPASy - ENZYME nomenclature database: 6.2.1.66
BRENDA, the Enzyme Database: 6.2.1.66

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