ID K6U0F4_9EURY Unreviewed; 514 AA.
AC K6U0F4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00282};
DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00282};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00282};
DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00282};
GN Name=pheS {ECO:0000256|HAMAP-Rule:MF_00282};
GN ORFNames=B655_1407 {ECO:0000313|EMBL:EKQ53257.1};
OS Methanobacterium sp. Maddingley MBC34.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=1220534 {ECO:0000313|EMBL:EKQ53257.1, ECO:0000313|Proteomes:UP000001147};
RN [1] {ECO:0000313|EMBL:EKQ53257.1, ECO:0000313|Proteomes:UP000001147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34 {ECO:0000313|Proteomes:UP000001147};
RX PubMed=23405289;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Midgley D.J.,
RA Hendry P.;
RT "Draft Genome Sequence of Methanobacterium sp. Maddingley, Reconstructed
RT from Metagenomic Sequencing of a Methanogenic Microbial Consortium Enriched
RT from Coal-Seam Gas Formation Water.";
RL Genome Announc. 1:E00082-12(2013).
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|HAMAP-Rule:MF_00282};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00282};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC Rule:MF_00282};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00006703, ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKQ53257.1}.
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DR EMBL; AMGN01000027; EKQ53257.1; -; Genomic_DNA.
DR AlphaFoldDB; K6U0F4; -.
DR STRING; 1220534.B655_1407; -.
DR PATRIC; fig|1220534.3.peg.1398; -.
DR eggNOG; arCOG00410; Archaea.
DR Proteomes; UP000001147; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00496; PheRS_alpha_core; 1.
DR Gene3D; 1.10.10.2320; -; 1.
DR Gene3D; 1.10.10.2330; -; 1.
DR Gene3D; 3.30.1370.240; -; 1.
DR HAMAP; MF_00282; Phe_tRNA_synth_alpha2; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR022917; Phe_tRNA_ligase_alpha_bac/arc.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00468; pheS; 1.
DR PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00282,
KW ECO:0000313|EMBL:EKQ53257.1};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00282};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00282};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00282, ECO:0000313|EMBL:EKQ53257.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00282};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00282}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00282};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00282}.
FT DOMAIN 257..506
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 354
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 392..394
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 431
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 457
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
SQ SEQUENCE 514 AA; 58381 MW; 6F7C21CE1A6B1FE7 CRC64;
MLDKIINEMH LYEKKVLKVL GEAGGQDIPE DVAKNTALDI KQVMSAAGAL ESKGIIEIER
DVEEVLSLGP SGSTYAQEGL PERKILEALH QDQTIHMKDL AQKSGIEPSE VKIAIGWIMK
KGWAVLDKGN VTITPNGEKA LEKPGIDEIL LKTIMDSTKI LTLGGLSNSL NEGFQQLKKR
KGLINLNKNS SYTLVVTKKG QDILDHGFEI REEATQLTHE QLKTDSWKNL HYRGYDIQAE
HPIIFPGKMH PLQRTIQEIR RIFLNLGFNE SRGTILESAF WNFDCLFQPQ DHAAREMQDT
FYVKSPRSTQ LPSDEMVKKV SQTHEDGGAT GSEGWGYHWD VDVAMQSVLR THTTCVSARY
LAENEPPLKM FSVGRVFRRE TITYKHLPEF HQVEGIVASE EINFKNLLGI IKEFYHQMGF
EVRFRPAYFP YTYLSTECEI YLPEKESWIE LGGSGMFRPE VLEPLGIETP VAAFGLGIER
LAMIRLGIKD IRMLYQSDLG WLRNLPVTQI YNEK
//
