ID A0A126R337_9SPHN Unreviewed; 804 AA.
AC A0A126R337;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283};
DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00283};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283};
DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00283};
GN Name=pheT {ECO:0000256|HAMAP-Rule:MF_00283,
GN ECO:0000313|EMBL:AMK16497.1};
GN ORFNames=K663_00520 {ECO:0000313|EMBL:AMK16497.1};
OS Sphingobium sp. MI1205.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=407020 {ECO:0000313|EMBL:AMK16497.1, ECO:0000313|Proteomes:UP000060707};
RN [1] {ECO:0000313|Proteomes:UP000060707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI1205 {ECO:0000313|Proteomes:UP000060707};
RA Tabata M.;
RT "Genome sequence of gamma-HCH degrading bacterium Sphingobium sp. MI1205.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMK16497.1, ECO:0000313|Proteomes:UP000060707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI1205 {ECO:0000313|EMBL:AMK16497.1,
RC ECO:0000313|Proteomes:UP000060707};
RX PubMed=27056230;
RA Tabata M., Ohhata S., Nikawadori Y., Sato T., Kishida K., Ohtsubo Y.,
RA Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of a gamma-Hexachlorocyclohexane-Degrading
RT Bacterium, Sphingobium sp. Strain MI1205.";
RL Genome Announc. 4:0-0(2016).
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:0000256|ARBA:ARBA00000395, ECO:0000256|HAMAP-
CC Rule:MF_00283};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00283};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC Rule:MF_00283};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00283}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00283}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000256|ARBA:ARBA00008653,
CC ECO:0000256|HAMAP-Rule:MF_00283}.
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DR EMBL; CP005188; AMK16497.1; -; Genomic_DNA.
DR RefSeq; WP_062112780.1; NZ_CP005188.1.
DR AlphaFoldDB; A0A126R337; -.
DR STRING; 407020.K663_00520; -.
DR KEGG; spmi:K663_00520; -.
DR PATRIC; fig|407020.3.peg.108; -.
DR OrthoDB; 9805455at2; -.
DR Proteomes; UP000060707; Chromosome 1.
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:UniProtKB-UniRule.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00769; PheRS_beta_core; 1.
DR CDD; cd02796; tRNA_bind_bactPheRS; 1.
DR Gene3D; 3.30.56.10; -; 2.
DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 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; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR033714; tRNA_bind_bactPheRS.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR NCBIfam; TIGR00472; pheT_bact; 1.
DR PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 1.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF54991; Anticodon-binding domain of PheRS; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF56037; PheT/TilS domain; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR PROSITE; PS51483; B5; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00283};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00283}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00283};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00283};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00283};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00283};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00209};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00209}.
FT DOMAIN 39..148
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT DOMAIN 397..486
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
FT DOMAIN 711..803
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00283"
SQ SEQUENCE 804 AA; 84883 MW; C217DFCB504540F8 CRC64;
MKFTLSWLKT HLTTDADLPT ILKGLTNIGL EVEGVENPAE KLAPFRIAKV LTADPHPQAD
KLQVLTVDAG DGALQVVCGA PNARAGLVGV FGTEGAVVPV NGMVLKKTAI RGVESNGMMC
SFRELELGED HDGIIELAPD APVGQVYAVW AGLDDPVIDV SITPNRQDCM GVRGIARDLA
AAGLGTLNPI IVPAIEGTGA GPDVRIEDAD GCPAFFARTV KGVRNGASPE WMAKRLTAIG
QKPISTLVDI TNYIMIDLGR PLHVYDLATL KGPLTARRGK PGEEVLALNG KTYTVDETMT
VIADDEAVHD IGGIMGGEHS GATEGTTDVL IECAYFTPER IAVTGQKLAL TSDARGRFER
GVDPAFLDDG LSIATYLVTE LCGGAPSEAT RAGSPPVADK IVIYEPSQCF ALAGVDVAED
EQRQILESLG FGVEGNDATF SYEDGMPVTT PANWTVKVPS WRRDVDGWPD LVEEVVRIVG
LDQVPSTPLP RAPGVAKATA TSEQLVERRV RRTAAARGLA EAINWSFISE KEAAAVGGGD
WTLANPISED LKVMRPSLLP GLLSAARRNM DRGAASVRLF ELGRRYFTSK ERATASFVLA
GEKVARGWQT GKAQPFSAYD AKAEVIALLA AAGAPVANLQ SFGEASAAYH PGQSGTLRLG
PKTVLAEFGV LHPSLAKQFG LTGAVVAGEI FLDAIPAKRA SGFMRAPYSP PALQAVKRDF
AFVVDDAVEA DALVRAVRNA DKKAIVDARL FDVFAGPGVD EGRKSLAVEV SLQPGEKSFS
QEELDAISAN IVKAAEKLGG TLRA
//
