SYS_METBF
ID SYS_METBF Reviewed; 423 AA.
AC Q46F20;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Serine--tRNA ligase;
DE EC=6.1.1.11;
DE AltName: Full=Seryl-tRNA synthetase;
DE Short=SerRS;
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
GN Name=serS1; OrderedLocusNames=Mbar_A0541;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [2]
RP FUNCTION, KINETIC PARAMETERS, AND TRNA(SER) RECOGNITION.
RX PubMed=15364939; DOI=10.1074/jbc.m408753200;
RA Korencic D., Polycarpo C., Weygand-Durasevic I., Soell D.;
RT "Differential modes of transfer RNA(Ser) recognition in Methanosarcina
RT barkeri.";
RL J. Biol. Chem. 279:48780-48786(2004).
CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able
CC to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-
CC seryl-tRNA(Sec), which will be further converted into selenocysteinyl-
CC tRNA(Sec). {ECO:0000269|PubMed:15364939}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 uM for L-serine {ECO:0000269|PubMed:15364939};
CC KM=13.8 uM for ATP {ECO:0000269|PubMed:15364939};
CC KM=2.9 uM for tRNA(Ser CGA) {ECO:0000269|PubMed:15364939};
CC KM=2.6 uM for tRNA(Ser GGA) {ECO:0000269|PubMed:15364939};
CC KM=1.3 uM for tRNA(Ser GCU) {ECO:0000269|PubMed:15364939};
CC Note=Catalytic efficiency is similar with the tRNA(Ser CGA) and
CC tRNA(Ser GGA) isoacceptors, but is 2-fold higher with tRNA(Ser GCU).;
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC terminal extension that is involved in tRNA binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ69522.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000099; AAZ69522.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048102491.1; NC_007355.1.
DR AlphaFoldDB; Q46F20; -.
DR SMR; Q46F20; -.
DR STRING; 269797.Mbar_A0541; -.
DR EnsemblBacteria; AAZ69522; AAZ69522; Mbar_A0541.
DR GeneID; 3627100; -.
DR KEGG; mba:Mbar_A0541; -.
DR eggNOG; arCOG00403; Archaea.
DR HOGENOM; CLU_023797_1_1_2; -.
DR OrthoDB; 16385at2157; -.
DR UniPathway; UPA00906; UER00895.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00770; SerRS_core; 1.
DR Gene3D; 1.10.287.40; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00176; Ser_tRNA_synth_type1; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR InterPro; IPR042103; SerRS_1_N_sf.
DR InterPro; IPR033729; SerRS_core.
DR InterPro; IPR010978; tRNA-bd_arm.
DR PANTHER; PTHR43697; PTHR43697; 1.
DR Pfam; PF02403; Seryl_tRNA_N; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00414; serS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..423
FT /note="Serine--tRNA ligase"
FT /id="PRO_0000285288"
FT BINDING 229..231
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT BINDING 258..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT BINDING 345..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
SQ SEQUENCE 423 AA; 48312 MW; 6F516EF31F695ADC CRC64;
MLDLKFVRSS PDIVRHALIN RNMSTELIDS LLEYDIAWRK CLTEGDELKH KRNVVTREIA
KLKKENKDTL SKIEEMQGIN SRIKEIDDII RDYKSKIHEI MLRIPNIPSS TTPVGKDEND
NPVVRIVGEP RKFTFTPKPH WEIGEALDIL DFEKGAKISG QGFTVYKGMG AKLERALVNF
MLEVHARQGY LEVFPPVLIN EKAMTGTGQL PKFKDDMYLC TDGYYLAPTA EVPVTNLFMD
DYIEKLPVFL TAYTACFRRE AGKHGQDTRG IIRQHQFNKV ELVKFVKPET SYDELEKLTN
DAEEILKLLK LPYRVVNLCT GDIGFSAAKT YDLEVWVPTQ EKYREISSCS NFENFQARRA
NIRFRTPDGP QFVHTLNGSG LAVGRTVVAI LENYQREDGS VEIPEVLRPY LGGAKEISNE
VKT
