ID H1Z369_9EURY Unreviewed; 459 AA.
AC H1Z369;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=Metlim_2436 {ECO:0000313|EMBL:EHQ36484.1};
OS Methanoplanus limicola DSM 2279.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoplanus.
OX NCBI_TaxID=937775 {ECO:0000313|EMBL:EHQ36484.1, ECO:0000313|Proteomes:UP000005741};
RN [1] {ECO:0000313|EMBL:EHQ36484.1, ECO:0000313|Proteomes:UP000005741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2279 {ECO:0000313|EMBL:EHQ36484.1,
RC ECO:0000313|Proteomes:UP000005741};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Wirth R., Brambilla E.-M., Klenk H.-P.,
RA Eisen J.A.;
RT "The Improved High-Quality Draft genome of Methanoplanus limicola DSM
RT 2279.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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; CM001436; EHQ36484.1; -; Genomic_DNA.
DR RefSeq; WP_004078803.1; NZ_CM001436.1.
DR AlphaFoldDB; H1Z369; -.
DR STRING; 937775.Metlim_2436; -.
DR PATRIC; fig|937775.9.peg.2750; -.
DR HOGENOM; CLU_060476_0_0_2; -.
DR InParanoid; H1Z369; -.
DR OrthoDB; 5817at2157; -.
DR Proteomes; UP000005741; 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 Reference proteome {ECO:0000313|Proteomes:UP000005741};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01675, ECO:0000313|EMBL:EHQ36484.1}.
FT BINDING 146..147
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT BINDING 251
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT BINDING 274..276
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT MOD_RES 277
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
SQ SEQUENCE 459 AA; 50283 MW; 2E904262C88A41D4 CRC64;
MNTRTSKTFE ALFALEDIRE VLRQALPTGP DAAEEAELKA GVARVRAILD DLEAGTGNVH
QPKIAGILDV RSREEEYINI QPIQAAGRLT PEARKALIAY GDGYSTCDAC RKPFRLDKIQ
KPPIAAFHED LAKFVNMDVA RVVPGARRGF QAVASSLVNK GDPVIVSGLS HYTEFLAVEG
AGGIVREVPI SKEHLVEPDR AAEKIEEVIR SDGKTPALMM IDHVDYQFAN IHDIKGLTKV
AHQYDIPFLC NGAYTVGVMP VDGKALGADF VVGSGHKSMA SPAPSGVLAT TDEWADIVFR
TTAMTGDVTN RKFGIKEVEM LGCTLMGGTL MAMMASFPAV RERTARFGEE VKKSNAFIKG
LLEIEGTEVL SEYPRKHTLS KVDTTGSFDK VAQVHKRRGF FLSDELKKRG IAGEFAGATR
AWKLNTYGLS WEKINYLTQA FQEIAEKYEI PVNKGHIQN
//
