ID SPSS2_METLZ Reviewed; 392 AA.
AC A2SSS7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=Mlab_1214;
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z;
RX PubMed=21304657; DOI=10.4056/sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(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; CP000559; ABN07383.1; -; Genomic_DNA.
DR RefSeq; WP_011833586.1; NC_008942.1.
DR AlphaFoldDB; A2SSS7; -.
DR SMR; A2SSS7; -.
DR STRING; 410358.Mlab_1214; -.
DR GeneID; 4795713; -.
DR KEGG; mla:Mlab_1214; -.
DR eggNOG; arCOG00091; Archaea.
DR HOGENOM; CLU_060476_0_0_2; -.
DR OrthoDB; 5817at2157; -.
DR Proteomes; UP000000365; 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 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; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..392
FT /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase 2"
FT /id="PRO_0000359454"
FT BINDING 85..86
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT BINDING 190
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT BINDING 213..215
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT MOD_RES 216
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
SQ SEQUENCE 392 AA; 42716 MW; 8D47B63C19D382A7 CRC64;
MKCAGQIEAR AVEESSINLD PIQAAGRLTP EAMKAVIAWG DGYSVCDNCH KPFRLDYVTK
PPIADFHEEA AKWLGMDKIQ LVPGARRAFQ EVTGALVGKG EPVIMTGMGH YTAYLSVEVV
NGVVREIRPT ADHHITADAA AESIENAVRE FGYAPKLVFV DAVDFMYGNM HEVEKIAKVA
HQYDIPVLYN GVYTVGVLPV DGKKLGVDFV VGSGHKSMAA PAPSGILATT DEYAEIVLRT
TKIQGDITGR KFGIKQVGIL GCSLMGDPAV GLIASFPRVK ERVNHFDEEL KNHKIVTDAL
LSIEGTKVAS EYPRKHTLTR MDTAGSFDVI ARTHKKRGFF LSSALNKRGI TGIMPGVTKQ
WKFNTYGLTK TQAEYLADSF IEIAEENSMV VG
//
