SPSS1_METHJ
ID SPSS1_METHJ Reviewed; 393 AA.
AC Q2FLN5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01675};
DE Short=SepCysS 1 {ECO:0000255|HAMAP-Rule:MF_01675};
GN OrderedLocusNames=Mhun_0071;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD39849.1; -; Genomic_DNA.
DR RefSeq; WP_011447146.1; NC_007796.1.
DR AlphaFoldDB; Q2FLN5; -.
DR SMR; Q2FLN5; -.
DR STRING; 323259.Mhun_0071; -.
DR EnsemblBacteria; ABD39849; ABD39849; Mhun_0071.
DR GeneID; 3923134; -.
DR KEGG; mhu:Mhun_0071; -.
DR eggNOG; arCOG00091; Archaea.
DR HOGENOM; CLU_060476_0_0_2; -.
DR OMA; HKSMAAS; -.
DR OrthoDB; 24071at2157; -.
DR Proteomes; UP000001941; 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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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:SF3; PTHR43586:SF3; 1.
DR Pfam; PF05889; SepSecS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR02539; SepCysS; 1.
PE 3: Inferred from homology;
KW Protein biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..393
FT /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase 1"
FT /id="PRO_0000359463"
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 393 AA; 42991 MW; 6B35901F6A8C11A1 CRC64;
MNCGEGIDSR QIDELFINLD PIQAGGRLTT DAMKAVLAYG DGYSVCDHCT KPFRLDHISK
PPLAEFHRDL ASFLNMDVAR LVPGARRGFQ AVASAMVKPG DPVLLTAYSH YTEFLSVEQS
KGTAFEIPAD ESHIITPDAA AARIEEVIKT TGKTPALMFI EQVDYQYGNQ HPVSDLSKVA
HQYDIPVLCN GAYTIGIMDV NGKELGADFL VGSGHKSMAA PAPSGVLATT SEWAEKVFRT
TGIKGDLTGR TFGVKEVEMM GCTLMGVTSV GMMASFPHVK RRVKEFDAQV QYVNRIVDAL
LTIEGTKVQS EYPRKHTLTR MNTTDSFDTV AKTHKKKGFF LTSALRERGI AGILPGSTRV
WKFNSYGITS EQADYIAESF IEIAEKEGLV CSR
