SPSS_METM5
ID SPSS_METM5 Reviewed; 380 AA.
AC A4FWT8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=MmarC5_0351;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000609; ABO34667.1; -; Genomic_DNA.
DR RefSeq; WP_011868122.1; NC_009135.1.
DR AlphaFoldDB; A4FWT8; -.
DR SMR; A4FWT8; -.
DR STRING; 402880.MmarC5_0351; -.
DR PRIDE; A4FWT8; -.
DR EnsemblBacteria; ABO34667; ABO34667; MmarC5_0351.
DR GeneID; 4929094; -.
DR KEGG; mmq:MmarC5_0351; -.
DR eggNOG; arCOG00091; Archaea.
DR HOGENOM; CLU_060476_0_0_2; -.
DR OMA; HKSMAAS; -.
DR OrthoDB; 24071at2157; -.
DR BRENDA; 2.5.1.73; 3262.
DR Proteomes; UP000000253; 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; Transferase.
FT CHAIN 1..380
FT /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase"
FT /id="PRO_0000359449"
FT BINDING 86..87
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT BINDING 192
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT BINDING 215..217
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT MOD_RES 218
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
SQ SEQUENCE 380 AA; 43395 MW; 61852827440F0C81 CRC64;
MEINTDKYKN ITRNLEREMI NLNPIQRGGI LPTESKKIIY EYWDGYSVCD YCSGRLDRIE
TPPINEFLED MSKFLGMDIT RPTHGARESK YAVMNSICKE GDYVVLDGNA HYTSYVAIER
AKLNYEKTDI GEYPTFRVIP ESYAEKIDML EDSKKNIGLI LLTHVDGNYG NVADVEKVGK
IAKSKGYPFL LNCAYSAGRM PIDGKKLNVD FIAASGHKSM AASGPCGLLS INKKYEDEVL
ETSKVNVVKE LQMLGCTSRG IPILSLMASF ERLIERVKKW DLELEKTRKV VNELEPLGFK
QIGEKPRNHD IIRFETPILD EIAEKDKRRG FFFYEELKRR GLGGIRRGVT KEFKMSVYGL
TNTQVDYVIN SMKTIINELR