SYFB_METTH
ID SYFB_METTH Reviewed; 549 AA.
AC O26864;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284};
DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00284};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284};
DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00284};
GN Name=pheT {ECO:0000255|HAMAP-Rule:MF_00284}; OrderedLocusNames=MTH_770;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP SUBUNIT.
RX PubMed=10575359; DOI=10.1016/s0300-9084(99)00332-6;
RA Das R., Vothknecht U.C.;
RT "Phenylalanyl-tRNA synthetase from the archaeon Methanobacterium
RT thermoautotrophicum is an (alphabeta)2 heterotetrameric protein.";
RL Biochimie 81:1037-1039(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00284};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00284};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00284, ECO:0000269|PubMed:10575359}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00284}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00284,
CC ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85273.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000666; AAB85273.1; ALT_INIT; Genomic_DNA.
DR PIR; A69203; A69203.
DR RefSeq; WP_010876408.1; NC_000916.1.
DR AlphaFoldDB; O26864; -.
DR SMR; O26864; -.
DR IntAct; O26864; 1.
DR STRING; 187420.MTH_770; -.
DR PRIDE; O26864; -.
DR EnsemblBacteria; AAB85273; AAB85273; MTH_770.
DR GeneID; 1471178; -.
DR KEGG; mth:MTH_770; -.
DR PATRIC; fig|187420.15.peg.758; -.
DR HOGENOM; CLU_020279_3_0_2; -.
DR OMA; FPGRCAN; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00769; PheRS_beta_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.50.40.10; -; 1.
DR HAMAP; MF_00284; Phe_tRNA_synth_beta2; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc_euk.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR022918; Phe_tRNA_ligase_beta2_arc.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR PANTHER; PTHR10947; PTHR10947; 1.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SUPFAM; SSF46955; SSF46955; 2.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00471; pheT_arch; 1.
DR PROSITE; PS51483; B5; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..549
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000127005"
FT DOMAIN 272..348
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284"
SQ SEQUENCE 549 AA; 61804 MW; D8F69E07C4E98B8A CRC64;
MPVITFDYDD LKELGIDIDR EKLLDVLPMM GSDIEDFDDE SIKVEFFPNR PDLLSVEGVA
RSLRGFLGIE KGMPSYDVHD SGVEVTVDES VLDVRPYLGM AVIEDVQFTD KKLKQVMEFQ
EDLHWVIGRD RRKVAIGIHD LDRVEPPFLY SGVEPEGVTF TPLDSVCEMT PHEILEEHPK
GVSYAHLLRD HDRYPLITDK NGDVLSMPPI INGELTKLTV NTRRILVDVT GTDDRAVRQT
LNIICTSFAE AGGRIGSVRV KRPDGELHLP DLTPREMRVS VSEASRITGL ELSADEVMDL
LMKARMDARR TSDDEVVAVI PAYRVDILHE VDLVENIAVQ HCIGRIEPEL PDIATIAEED
TWSRADASIR EVMVGLGFQE VMSLMLTSEE SHYRRMRLEE DERVEVAQPI SQDRTMIRKS
LLNGLLEFFE DNKHEDLPQK IFEVGDVVYI NPESETRSRV VTKLACAVTH SSAGFTEIKS
LAAAVVENLG YEFRIEPLEH PSFIEGRCAA IESEGKSSAI GGFFGEVHPE VVTNFNLEYP
VIALEIEFK
