ID K0I0Z1_9BURK Unreviewed; 438 AA.
AC K0I0Z1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Serine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00176};
DE EC=6.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00176};
DE AltName: Full=Seryl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
DE Short=SerRS {ECO:0000256|HAMAP-Rule:MF_00176};
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
GN Name=serS {ECO:0000256|HAMAP-Rule:MF_00176};
GN ORFNames=C380_05595 {ECO:0000313|EMBL:AFU44834.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU44834.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU44834.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU44834.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(2012).
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:0000256|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:0000256|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:0000256|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:0000256|ARBA:ARBA00005045, ECO:0000256|HAMAP-Rule:MF_00176}.
CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
CC {ECO:0000256|HAMAP-Rule:MF_00176}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00176}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00176}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00176}.
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DR EMBL; CP003872; AFU44834.1; -; Genomic_DNA.
DR RefSeq; WP_015012912.1; NC_018708.1.
DR AlphaFoldDB; K0I0Z1; -.
DR STRING; 358220.C380_05595; -.
DR KEGG; ack:C380_05595; -.
DR PATRIC; fig|358220.3.peg.1148; -.
DR eggNOG; COG0172; Bacteria.
DR HOGENOM; CLU_023797_1_1_4; -.
DR OrthoDB; 9804647at2; -.
DR UniPathway; UPA00906; UER00895.
DR Proteomes; UP000006306; 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00176};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00176}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00176};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00176};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00176}.
FT DOMAIN 175..423
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT COILED 33..60
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 245..247
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT BINDING 276..278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT BINDING 299
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT BINDING 363..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT BINDING 398
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
SQ SEQUENCE 438 AA; 48231 MW; 0822A460954D793F CRC64;
MLDILLLRKD LDTAIARLET RKKPQAFLDV SAFQALESER KTLQTRTEEL QAQRNQLSKQ
VGMLMSRGDK DGAEAVKAQV AAGKVELEQS AARLEQIQSE LLAMLVAVPN LPHESVPVGS
DEAGNVEVRR WGTPAKFDFE VKDHVDVGTP LGLDFDMGVK LSGSRFTVMK GSIARLHRAL
SQFMLDVQTQ EHGYTECYVP YAVNADSLKG TGQLPKFEGD LFAAKKGGQD GEPVPDNAAL
YLIPTSEVPL TNFVRDVVVA EADLPIKLTA HTPCFRSEAG SYGRDTRGMI RQHQFDKVEM
VQIVHPDKSY EALEEMTRHA ETVLQKLGLP YRVMSLCTGD MGFGAAKTYD LEVWLPAQNT
YREISSVSNC EAFQARRLQA RFKNAQGKNE LLHTLNGSGL AVGRTLVAVL ENYQQADGSV
TVPEVLRPYL GGTAVLKP
//
