ID SYS_GLUOX Reviewed; 420 AA. AC Q5FQ48; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00176}; DE EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00176}; DE Short=SerRS {ECO:0000255|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_00176}; GN Name=serS {ECO:0000255|HAMAP-Rule:MF_00176}; GN OrderedLocusNames=GOX1759; OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=290633; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=621H; RX PubMed=15665824; DOI=10.1038/nbt1062; RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., RA Ehrenreich A., Gottschalk G., Deppenmeier U.; RT "Complete genome sequence of the acetic acid bacterium Gluconobacter RT oxydans."; RL Nat. Biotechnol. 23:195-200(2005). 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:0000255|HAMAP-Rule:MF_00176}. 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00176}; 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00176}; CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N- CC terminal extension that is involved in tRNA binding. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00176}. 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; CP000009; AAW61498.1; -; Genomic_DNA. DR RefSeq; WP_011253279.1; NZ_LT900338.1. DR AlphaFoldDB; Q5FQ48; -. DR SMR; Q5FQ48; -. DR STRING; 290633.GOX1759; -. DR KEGG; gox:GOX1759; -. DR eggNOG; COG0172; Bacteria. DR HOGENOM; CLU_023797_1_1_5; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000006375; Chromosome. 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:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00770; SerRS_core; 1. DR Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 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 NCBIfam; TIGR00414; serS; 1. DR PANTHER; PTHR43697:SF1; SERINE--TRNA LIGASE; 1. DR PANTHER; PTHR43697; SERYL-TRNA SYNTHETASE; 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; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF46589; tRNA-binding arm; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..420 FT /note="Serine--tRNA ligase" FT /id="PRO_0000122055" FT BINDING 229..231 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 260..262 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 283 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 347..350 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 381 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" SQ SEQUENCE 420 AA; 46055 MW; 988A253829198B49 CRC64; MHDLKALRAD PAAFDAALAR RGLSPVGQQL VSDDEGRRAA LAALQEAQGA RKALAKEIGL LKRQKLDTAE IEAKAVALRD QIAGLEERAN TIQTRIDDVL KSLPNCLDAS VPDGKGEDEN VVVHVRGEKR EFAFEAKQHF ELGEALGLMD FPTAAKLSGT RFVVLRGALA RLERALGQFM LDTHTTEFGY SETSVPLLVN DDAMYGTDKL PKFAEDSFRT EDGRWLIPTA EVPLTASVMG EILPADALPI RMTALSQCFR SEAGSAGRDV RGMLRQHQFT KCELVSVVKP EDSDAEHERM TQAAETVLER LGITFRRMLL CAGDTGFGAA KTFDLEAWLP GQKAWREISS CSNTRDFQAR RMNARYRAEN GPAFVNTLNG SGLAVGRTMI AVMETYQNED GSIDIPEVLR PYMGGLNRIG //