ID D1YWV7_METPS Unreviewed; 384 AA.
AC D1YWV7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase {ECO:0000256|HAMAP-Rule:MF_01675};
DE EC=2.5.1.73 {ECO:0000256|HAMAP-Rule:MF_01675};
DE AltName: Full=Sep-tRNA:Cys-tRNA synthase {ECO:0000256|HAMAP-Rule:MF_01675};
DE Short=SepCysS {ECO:0000256|HAMAP-Rule:MF_01675};
GN OrderedLocusNames=MCP_0857 {ECO:0000313|EMBL:BAI60929.1};
OS Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS SANAE).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60929.1, ECO:0000313|Proteomes:UP000001882};
RN [1] {ECO:0000313|Proteomes:UP000001882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC {ECO:0000313|Proteomes:UP000001882};
RX PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA Mori K., Fujita N., Imachi H., Takai K.;
RT "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT paludicola, the first cultivated representative of the order
RT Methanocellales.";
RL PLoS ONE 6:E22898-E22898(2011).
CC -!- FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-
CC cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). {ECO:0000256|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:0000256|HAMAP-Rule:MF_01675};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01675};
CC -!- SUBUNIT: Homodimer. Interacts with SepRS. {ECO:0000256|HAMAP-
CC Rule:MF_01675}.
CC -!- SIMILARITY: Belongs to the SepCysS family. {ECO:0000256|HAMAP-
CC Rule:MF_01675}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP011532; BAI60929.1; -; Genomic_DNA.
DR AlphaFoldDB; D1YWV7; -.
DR STRING; 304371.MCP_0857; -.
DR KEGG; mpd:MCP_0857; -.
DR PATRIC; fig|304371.9.peg.882; -.
DR eggNOG; arCOG00091; Archaea.
DR InParanoid; D1YWV7; -.
DR Proteomes; UP000001882; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR02539; SepCysS; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF3; O-PHOSPHO-L-SERYL-TRNA:CYS-TRNA SYNTHASE; 1.
DR Pfam; PF05889; SepSecS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01675}; Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01675};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01675}.
FT BINDING 88..89
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT BINDING 195
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT BINDING 218..220
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT MOD_RES 221
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
SQ SEQUENCE 384 AA; 42392 MW; 892167EFF84E875A CRC64;
MCMAINTAKF GFIKRDTPRE INLDPLQTGG ILTPEARQAL QEWGDGYSVC DYCGGALDQI
KTPPIFDFIN KALPEFLGCD QARVTNGARE AKFAVMHAVC KEGDWVVMDG NAHYSSLVAA
QRARLNIKLV EKTPAPEYKI LPEKYAEAID AVKRESGRAP ALALLTYPDG SYGNIADAKA
ISKIVHDNGI PFLVNGAYAI GRMPFNAKEL GADFVSGSGH KSMASSGPIG VLGVSNQYAP
KVLAKSPTNK NKEIEFLGCT ARGATIMTML ASFPAVYERT RPERWQKEVE DARWFSGQLE
SLGLKQLGDK PHDHDLMFFE SMPFYDISQK ADRYFLYREM KARSIHGIKP GLTKNFKLST
FGVGREKLGI VVDAFKEILQ KYST
//
