KEGG   ENZYME: 6.2.2.1
Entry
EC 6.2.2.1                  Enzyme                                 

Name
thioglycine synthase;
ycaO (gene name) (ambiguous)
Class
Ligases;
Forming carbon-sulfur bonds;
Amide---thiol ligases
Sysname
[methyl-coenzyme M reductase]-glycine---sulfur ligase (thioglycine-forming)
Reaction(IUBMB)
ATP + sulfide + a [methyl-coenzyme M reductase]-glycine = ADP + phosphate + a [methyl-coenzyme M reductase]-thioglycine
Substrate
ATP [CPD:C00002];
sulfide [CPD:C00283];
[methyl-coenzyme M reductase]-glycine
Product
ADP [CPD:C00008];
phosphate [CPD:C00009];
[methyl-coenzyme M reductase]-thioglycine
Comment
Requires Mg2+. The enzyme is found in anaerobic methanogenic and methanotrophic archaea, where it modifies a glycine residue in EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase (methyl-CoM reductase). Upon binding to its substrate, an external source of sulfide attacks the target amide bond generating a tetrahedral intermediate. The amide oxyanion attacks the gamma-phosphate of ATP, releasing ADP and forming a phosphorylated thiolate intermediate that collapses to form thioglycine and phosphate. In most organisms activity requires a second protein (TfuA) , which may allosterically activate this enzyme or assist in the delivery of sulfide to the substrate.
History
EC 6.2.2.1 created 2020
Orthology
K24409  thioglycine synthase
Genes
PFUW: KF707C_3290
DLI: dnl_33670
MFB: MFUL124B02_11525 MFUL124B02_15270
AVM: JQX13_45925
RII: FFM53_031610
RBAN: J2J98_24555
STAR: G3545_06705
LIZ: LGH83_15860
LCK: HN018_08740
AOZ: HUE56_13285
PCOR: KS4_05530
MJA: MJ_1094
MMP: MMP1056
MMD: GYY_06120
MMAD: MMJJ_17940
MAE: Maeo_0842
MVO: Mvol_0253
MTH: MTH_987
METC: MTCT_0897
METE: tca_00950
MST: Msp_1155
MRU: mru_0668
MSI: Msm_0480
MEB: Abm4_0398
MMIL: sm9_0538
MEYE: TL18_02440
MOL: YLM1_0309
METH: MBMB1_1575
MFC: BRM9_0810
MCUB: MCBB_1870
MFV: Mfer_0482
MBAR: MSBR2_2206
MBAK: MSBR3_2262
MAC: MA_0165
MMA: MM_1458
MMAC: MSMAC_3228
METM: MSMTP_3106
MTHR: MSTHT_1941
MTHE: MSTHC_1342
MHOR: MSHOH_3957
MBU: Mbur_2069
MMET: MCMEM_0269
MMH: Mmah_0267
MPY: Mpsy_2233
MTP: Mthe_1401
MCJ: MCON_2772
MHI: Mhar_1259
MHU: Mhun_0527
MLA: Mlab_0591
MEMA: MMAB1_2861
MPI: Mpet_0085
MBN: Mboo_1978
MPL: Mpal_1211
MPD: MCP_0554
MEZ: Mtc_0967
RCI: RCIX2079
MARC: AR505_1405
NEV: NTE_02802
NCV: NCAV_1569
 » show all
Reference
1  [PMID:28880150]
  Authors
Nayak DD, Mahanta N, Mitchell DA, Metcalf WW.
  Title
Post-translational thioamidation of methyl-coenzyme M reductase, a key enzyme in  methanogenic and methanotrophic Archaea.
  Journal
Elife 6:e29218 (2017)
DOI:10.7554/eLife.29218
  Sequence
Reference
2  [PMID:29507203]
  Authors
Mahanta N, Liu A, Dong S, Nair SK, Mitchell DA
  Title
Enzymatic reconstitution of ribosomal peptide backbone thioamidation.
  Journal
Proc Natl Acad Sci U S A 115:3030-3035 (2018)
DOI:10.1073/pnas.1722324115
  Sequence
[mac:MA_0165 MA_0164] [mka:MK0115]
Reference
3  [PMID:31139720]
  Authors
Dong SH, Liu A, Mahanta N, Mitchell DA, Nair SK
  Title
Mechanistic Basis for Ribosomal Peptide Backbone Modifications.
  Journal
ACS Cent Sci 5:842-851 (2019)
DOI:10.1021/acscentsci.9b00124
  Sequence
[mja:MJ_1094]
Other DBs
ExplorEnz - The Enzyme Database: 6.2.2.1
IUBMB Enzyme Nomenclature: 6.2.2.1
ExPASy - ENZYME nomenclature database: 6.2.2.1
BRENDA, the Enzyme Database: 6.2.2.1

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