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Database: UniProt
Entry: A0A0P9E813_9ARCH
LinkDB: A0A0P9E813_9ARCH
Original site: A0A0P9E813_9ARCH 
ID   A0A0P9E813_9ARCH        Unreviewed;       393 AA.
AC   A0A0P9E813;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   ORFNames=AOA66_0045 {ECO:0000313|EMBL:KPV64612.1};
OS   Candidatus Bathyarchaeota archaeon BA2.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1700836 {ECO:0000313|EMBL:KPV64612.1, ECO:0000313|Proteomes:UP000050284};
RN   [1] {ECO:0000313|EMBL:KPV64612.1, ECO:0000313|Proteomes:UP000050284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA2 {ECO:0000313|EMBL:KPV64612.1};
RX   PubMed=26494757; DOI=10.1126/science.aac7745;
RA   Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA   Golding S.D., Tyson G.W.;
RT   "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT   genome-centric metagenomics.";
RL   Science 350:434-438(2015).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPV64612.1}.
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DR   EMBL; LIHK01000002; KPV64612.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P9E813; -.
DR   STRING; 1700836.AOA66_0045; -.
DR   KEGG; barb:AOA66_0045; -.
DR   Proteomes; UP000050284; Unassembled WGS sequence.
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|HAMAP-Rule:MF_01675};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01675};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01675}.
FT   BINDING         86..87
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT   BINDING         191
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT   BINDING         214..216
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT   MOD_RES         217
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
SQ   SEQUENCE   393 AA;  44149 MW;  185F7EEC76EF50B8 CRC64;
     MKQMIEEIEV RAREELFINI QPIQAAGRLT PEAMKAIIAY GDGYSTCDWC MAPFRLDKIR
     MPPINEFHVK LAKFVGMDQA RVVPGARRGF QAVVSSLVEK GDSVIVSALA HYTEFLAVEN
     VGGIVKEVPL NEENIVTGEN TAQKIEKVKK ETGKLPKLIM MDHFDYMFGN EHDIHGIAKV
     AKEYDVPFLA NCAYSLGVMP VNGKEMGADF LVGSGHKSFA SPAPSGILAT TNEWAEKVFR
     TTQMVGDLTG RKFGIKEVEM MGCTLMGANL IAMMASFPAV HERVKHWDDE IKKANYFIDE
     FLKIEGNKVL SEMPRKHTLT KVDTTGSFDK IARTHKRRGF FFSDELKKRR IIGEFAGATR
     QWKLNTYGLT WDQIKYLAEA FQDIAKKYGM NVA
//
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