AC MF_01675; DC Protein; auto TR HAMAP; MF_01675; -; 1; level=0 XX Names: Sep_Cys_tRNA_synth XX ID SPSS DE RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase; DE EC=2.5.1.73; DE AltName: Full=Sep-tRNA:Cys-tRNA synthase; DE Short=SepCysS; XX CC -!- FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L- CC cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L- CC cysteinyl-tRNA(Cys) + phosphate; Xref=Rhea:RHEA:25686, Rhea:RHEA- CC COMP:9679, Rhea:RHEA-COMP:9719, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:78517, ChEBI:CHEBI:78551; EC=2.5.1.73; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- SUBUNIT: Homodimer. Interacts with SepRS. CC -!- SIMILARITY: Belongs to the SepCysS family. XX DR Pfam; PF05889; SLA_LP_auto_ag; 1; trigger=no DR NCBIfam; TIGR02539; SepCysS; 1; trigger=no XX KW Protein biosynthesis KW Pyridoxal phosphate KW Transferase XX GO GO:0043766; F:Sep-tRNA:Cys-tRNA synthase activity XX FT From: SPSS1_ARCFU (O30207) FT BINDING 78..79 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT Condition: A-R FT BINDING 206..208 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT Condition: S-G-H FT BINDING 183 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT Condition: N FT MOD_RES 209 FT /note="N6-(pyridoxal phosphate)lysine" FT Condition: K XX Size: 371-463; Related: None; Template: Q59072; O30207; Scope: Archaea Fusion: Nter: None Cter: None Duplicate: in ARCFU, METB6, METBU, METHJ, METLZ, METAR Plasmid: None Comments: Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus and Methanopyrus kandleri use the SepRS?SepCysS pathway obligatorily for synthesis of Cys-tRNACys, whereas many others (for example, Methanococcus maripaludis and Archaeoglobus fulgidus) contain genes for both the CysRS and the SepRS?SepCysS pathways (PMID:16380427). XX # Revision 1.18 2023/06/01 //