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
//