SPSS_METTH
ID SPSS_METTH Reviewed; 377 AA.
AC O27139;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=MTH_1067;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB85556.1; -; Genomic_DNA.
DR PIR; F69008; F69008.
DR RefSeq; WP_010876691.1; NC_000916.1.
DR AlphaFoldDB; O27139; -.
DR SMR; O27139; -.
DR STRING; 187420.MTH_1067; -.
DR EnsemblBacteria; AAB85556; AAB85556; MTH_1067.
DR GeneID; 24854199; -.
DR KEGG; mth:MTH_1067; -.
DR PATRIC; fig|187420.15.peg.1044; -.
DR HOGENOM; CLU_060476_0_0_2; -.
DR OMA; HKSMAAS; -.
DR Proteomes; UP000005223; 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..377
FT /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase"
FT /id="PRO_0000107476"
FT BINDING 83..84
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT BINDING 188
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT BINDING 211..213
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT MOD_RES 214
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
SQ SEQUENCE 377 AA; 42022 MW; 24C0EE1FA77C7AE4 CRC64;
MECADYGLTR KLERDNLNLN PLQRGGVLPA AARKALHEFG DGYSVCDYCD GRLDQVTRPA
INCFLDDLAD FTGSDAVRTV HGAREGKFAV MHALCERGDT VVVDGNAHYT THLAAERNGL
EIVEVPSTGH PSYEVTPEAY REVLEETIDR VEVKLAVLTH VDGNYGNLTD ARGVADVCRK
LGVPLLLNCA YSMGRLPVNL RELGVDFVVG SGHKSMAASG PIGVLGMKSE WEDTVLRRSG
RHEKKELELL GCTSRGAPLA TLMASLPYVR ERVSRWDGEV KKTRYLVSEL EDIGGIEQLG
VRPKEHDLVR FETPVFHEIA ASHPRKGFFL YEELKKRGIV GIRRGQTKWF KCSIYGMTEE
QVQYVVDSFR DIVEENR
