ID   SPSS_METBF              Reviewed;         386 AA.
AC   Q46C09;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Mbar_A1638;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ70583.1; -; Genomic_DNA.
DR   RefSeq; WP_011306629.1; NC_007355.1.
DR   AlphaFoldDB; Q46C09; -.
DR   SMR; Q46C09; -.
DR   STRING; 269797.Mbar_A1638; -.
DR   EnsemblBacteria; AAZ70583; AAZ70583; Mbar_A1638.
DR   GeneID; 3625436; -.
DR   KEGG; mba:Mbar_A1638; -.
DR   eggNOG; arCOG00091; Archaea.
DR   HOGENOM; CLU_060476_0_0_2; -.
DR   OMA; HKSMAAS; -.
DR   OrthoDB; 24071at2157; -.
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; Transferase.
FT   CHAIN           1..386
FT                   /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase"
FT                   /id="PRO_0000359461"
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;  42705 MW;  D922AF7ADC953E7A CRC64;
     MKLDDSSLQK FGFIKRDTLG SINIDPLQTG GRLTEAAKQA LVEWGDGYSV CDFCGGILDQ
     IKKPPIYDFV HKALPEFLDC DEARVTNGAR ESKFAVMHSI GKPGDWIVLD GLAHYSSYVA
     AERAGLNIKT VPHSGSPDYY LDPEGYATAI EEVTKESGKP PALALVTYPD GSYGNLPDAR
     KIASVCHEYD VPLLLNGAYA VGRMPVSAKE IGADFIAGSG HKSMAASGPV GVLGVSEEYA
     PIVFRKSKYN KVKEVELLGC TARGATVMTL IASFPDVVKR VRNWDQEVEN ARWFSARFEE
     MGFIQRGQKP HSHDLMFFEA PRFYEISEKV KKGRYFLYKD LKARNIHGIK SGLTKYFKLS
     TFGLGKEKLG IVADSFEEIL KKYEDV