ID   SPSS2_METB6             Reviewed;         454 AA.
AC   A7I9Z8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Mboo_2045;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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; CP000780; ABS56559.1; -; Genomic_DNA.
DR   RefSeq; WP_012107615.1; NC_009712.1.
DR   AlphaFoldDB; A7I9Z8; -.
DR   SMR; A7I9Z8; -.
DR   STRING; 456442.Mboo_2045; -.
DR   PRIDE; A7I9Z8; -.
DR   EnsemblBacteria; ABS56559; ABS56559; Mboo_2045.
DR   GeneID; 5410678; -.
DR   KEGG; mbn:Mboo_2045; -.
DR   eggNOG; arCOG00091; Archaea.
DR   HOGENOM; CLU_060476_0_0_2; -.
DR   OMA; WKLNTYG; -.
DR   OrthoDB; 24071at2157; -.
DR   Proteomes; UP000002408; 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..454
FT                   /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase 2"
FT                   /id="PRO_0000359458"
FT   BINDING         146..147
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         251
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         274..276
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
SQ   SEQUENCE   454 AA;  50084 MW;  83F825D0A706300E CRC64;
     MSIRVQKTFE ALFELEEIRG IFRDSLPTGL SAEEEAAFRQ RIGNLKAIVA DLEAGTGTPK
     VTKIAGTLDV RSREEQYINI HPIQAAGRLT TEARKAIISY GDGYSTCDAC RKPFRLDKIS
     KPGIAEFHAD LAKWLNMDHA RVVPGARRGF QAVTGTLVNK GDSVIVSALA HYTEFLSVEN
     AGGVIKEVPL NAKNIVTGEA TAQKIEEVKT ETGKLPVLVM IDHFDYQFAN EHEIREIGKV
     AHQYDIPFLY NGAYTVGVQP VDGKKIGADF VVGSGHKSMA SVAPSGVLAT TKEWAPKALR
     TTAIVGDLTK RKFGIKEVEL LGCTLMGGTL LSMIASFPAV KERVLHWDEQ VKRSNYFIDR
     LLKISGSRVL SEYPRRHTLT KVDTTGSFDT VAKTHKRRGF YFSDELSSRG IVGEFAGATR
     TWKLNTYGLS EKQVHYLADA FTEIAEKFEL PVTK