SPSS2_METBU
ID SPSS2_METBU Reviewed; 387 AA.
AC Q12W26;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Mbur_1440;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(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; CP000300; ABE52350.1; -; Genomic_DNA.
DR RefSeq; WP_011499495.1; NC_007955.1.
DR AlphaFoldDB; Q12W26; -.
DR SMR; Q12W26; -.
DR STRING; 259564.Mbur_1440; -.
DR EnsemblBacteria; ABE52350; ABE52350; Mbur_1440.
DR GeneID; 3998468; -.
DR KEGG; mbu:Mbur_1440; -.
DR HOGENOM; CLU_060476_0_0_2; -.
DR OMA; HKSMAAS; -.
DR OrthoDB; 24071at2157; -.
DR BRENDA; 2.5.1.73; 9200.
DR Proteomes; UP000001979; 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..387
FT /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase 2"
FT /id="PRO_0000359446"
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 387 AA; 42984 MW; 35B34C4FFF69373A CRC64;
MTLDDAALKS FGFIERPTKN MINIDPLQTG GILTEDARRA LVEWGDGYSI CDNCGGVLDL
IKKPPVQKFI HEALPEFLGV DEVRITHGAR ESKFAVMHAI AQEGDTVILD GLAHYSSVVA
AQRARLEIRK VPHSEKPDYH IDPEAYGTAI EETISETGKA PALALLTYPD GNYGNLADAK
KIASVCHEYD VPLLLNCAYS VGRMPVDAKE LGVDFIAGSG HKSMASCGPI GVLGVNNDNG
DYSDIIFRKS PTNKNKEIEL LGCTARSATL MTMIASFPEV VKRTRNWGNE VADARWFSEK
LETMGLIQMG QKPHNHDLMF FEAPNLYEIS TRVKKGRYFL YKELKSRNIH GIKAGLTKFF
KLSTFEVGRE NLSYIVDSFD EIIKKYE
