ID   SPSS2_METLZ             Reviewed;         392 AA.
AC   A2SSS7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01675};
DE            Short=SepCysS 2 {ECO:0000255|HAMAP-Rule:MF_01675};
GN   OrderedLocusNames=Mlab_1214;
OS   Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX   NCBI_TaxID=410358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43576 / DSM 4855 / Z;
RX   PubMed=21304657; DOI=10.4056/sigs.35575;
RA   Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL   Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN07383.1; -; Genomic_DNA.
DR   RefSeq; WP_011833586.1; NC_008942.1.
DR   AlphaFoldDB; A2SSS7; -.
DR   SMR; A2SSS7; -.
DR   STRING; 410358.Mlab_1214; -.
DR   EnsemblBacteria; ABN07383; ABN07383; Mlab_1214.
DR   GeneID; 4795713; -.
DR   KEGG; mla:Mlab_1214; -.
DR   eggNOG; arCOG00091; Archaea.
DR   HOGENOM; CLU_060476_0_0_2; -.
DR   OMA; HHITADA; -.
DR   OrthoDB; 24071at2157; -.
DR   Proteomes; UP000000365; 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.
PE   3: Inferred from homology;
KW   Protein biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..392
FT                   /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase 2"
FT                   /id="PRO_0000359454"
FT   BINDING         85..86
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         190
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         213..215
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   MOD_RES         216
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
SQ   SEQUENCE   392 AA;  42716 MW;  8D47B63C19D382A7 CRC64;
     MKCAGQIEAR AVEESSINLD PIQAAGRLTP EAMKAVIAWG DGYSVCDNCH KPFRLDYVTK
     PPIADFHEEA AKWLGMDKIQ LVPGARRAFQ EVTGALVGKG EPVIMTGMGH YTAYLSVEVV
     NGVVREIRPT ADHHITADAA AESIENAVRE FGYAPKLVFV DAVDFMYGNM HEVEKIAKVA
     HQYDIPVLYN GVYTVGVLPV DGKKLGVDFV VGSGHKSMAA PAPSGILATT DEYAEIVLRT
     TKIQGDITGR KFGIKQVGIL GCSLMGDPAV GLIASFPRVK ERVNHFDEEL KNHKIVTDAL
     LSIEGTKVAS EYPRKHTLTR MDTAGSFDVI ARTHKKRGFF LSSALNKRGI TGIMPGVTKQ
     WKFNTYGLTK TQAEYLADSF IEIAEENSMV VG