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SPSS_METMA
ID   SPSS_METMA              Reviewed;         386 AA.
AC   Q8PVS9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase {ECO:0000255|HAMAP-Rule:MF_01675};
DE            EC=2.5.1.73 {ECO:0000255|HAMAP-Rule:MF_01675};
DE   AltName: Full=Sep-tRNA:Cys-tRNA synthase {ECO:0000255|HAMAP-Rule:MF_01675};
DE            Short=SepCysS {ECO:0000255|HAMAP-Rule:MF_01675};
GN   OrderedLocusNames=MM_1881;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC   -!- FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-
CC       cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). {ECO:0000255|HAMAP-Rule:MF_01675}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01675};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01675};
CC   -!- SUBUNIT: Homodimer. Interacts with SepRS. {ECO:0000255|HAMAP-
CC       Rule:MF_01675}.
CC   -!- SIMILARITY: Belongs to the SepCysS family. {ECO:0000255|HAMAP-
CC       Rule:MF_01675}.
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DR   EMBL; AE008384; AAM31577.1; -; Genomic_DNA.
DR   RefSeq; WP_011033816.1; NC_003901.1.
DR   AlphaFoldDB; Q8PVS9; -.
DR   SMR; Q8PVS9; -.
DR   STRING; 192952.MM_1881; -.
DR   EnsemblBacteria; AAM31577; AAM31577; MM_1881.
DR   GeneID; 1480223; -.
DR   KEGG; mma:MM_1881; -.
DR   PATRIC; fig|192952.21.peg.2168; -.
DR   eggNOG; arCOG00091; Archaea.
DR   HOGENOM; CLU_060476_0_0_2; -.
DR   OMA; HKSMAAS; -.
DR   BRENDA; 2.5.1.73; 3270.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0043766; F:Sep-tRNA:Cys-tRNA synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01675; Sep_Cys_tRNA_synth; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR013375; Sep_Cys-tRNA_synth_arc.
DR   InterPro; IPR008829; SepSecS/SepCysS.
DR   PANTHER; PTHR43586:SF3; PTHR43586:SF3; 1.
DR   Pfam; PF05889; SepSecS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02539; SepCysS; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..386
FT                   /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase"
FT                   /id="PRO_0000359462"
FT   BINDING         89..90
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         196
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         219..221
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   MOD_RES         222
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
SQ   SEQUENCE   386 AA;  42324 MW;  0D15575C06A1ED55 CRC64;
     MTLDDSSLQK FGFIKRETLG SINIDPLQTG GLLTGAAKQA LVEWGDGYSV CDFCGGVLDL
     VKKPPIHDFV HKALPEFLGC DEARVTNGAR ESKFAVMHSM GKPGDWVVLD GLAHYSSYVA
     AERAGLNIEV VPHAGSPEYH LDPGRYGKAI EEVTKENGKP PVLALVTYPD GSYGNIPDAA
     KIASVCHEYD VPLLLNGAYS VGRMPVSAKE IGADFIVGSG HKSMAASGPV GVLGVSEEYA
     PVVFRKSVHN KVKEIELLGC TARGATVMTL MASFPEVVKR TRNWDQEVEN ARWFSSRLEG
     MGFIQRGQKP HSHDLMFFEA PGFYEISQKV KNGRYFLYRE LKERNIHGIK SGLTKYFKLS
     TFGLGKEKLG TVADAFEDIL KKYENI
 
 
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