ID F9Z3Z2_ODOSD Unreviewed; 339 AA.
AC F9Z3Z2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00281};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00281};
GN Name=pheS {ECO:0000256|HAMAP-Rule:MF_00281};
GN OrderedLocusNames=Odosp_2638 {ECO:0000313|EMBL:ADY33618.1};
OS Odoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / CIP 104287 / JCM
OS 15291 / NCTC 10825 / 1651/6) (Bacteroides splanchnicus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC Odoribacter.
OX NCBI_TaxID=709991 {ECO:0000313|EMBL:ADY33618.1, ECO:0000313|Proteomes:UP000006657};
RN [1] {ECO:0000313|EMBL:ADY33618.1, ECO:0000313|Proteomes:UP000006657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6
RC {ECO:0000313|Proteomes:UP000006657};
RX PubMed=21677857; DOI=10.4056/sigs.1714269;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Goker M., Gronow S., Zeytun A., Nolan M., Lucas S., Lapidus A., Hammon N.,
RA Deshpande S., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA Rohde M., Detter J.C., Woyke T., Bristow J., Markowitz V., Hugenholtz P.,
RA Eisen J.A., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Odoribacter splanchnicus type strain
RT (1651/6).";
RL Stand. Genomic Sci. 4:200-209(2011).
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_00281};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00281};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC Rule:MF_00281};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00281}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00281}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00010207, ECO:0000256|HAMAP-Rule:MF_00281}.
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DR EMBL; CP002544; ADY33618.1; -; Genomic_DNA.
DR RefSeq; WP_013612811.1; NZ_CP086000.1.
DR AlphaFoldDB; F9Z3Z2; -.
DR STRING; 709991.Odosp_2638; -.
DR PaxDb; 709991-Odosp_2638; -.
DR GeneID; 69854968; -.
DR KEGG; osp:Odosp_2638; -.
DR eggNOG; COG0016; Bacteria.
DR HOGENOM; CLU_025086_0_1_10; -.
DR OrthoDB; 9800719at2; -.
DR BioCyc; OSPL709991:G1GRN-2686-MONOMER; -.
DR Proteomes; UP000006657; 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: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 HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 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; IPR004188; Phe-tRNA_ligase_II_N.
DR InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR010978; tRNA-bd_arm.
DR NCBIfam; TIGR00468; pheS; 1.
DR PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
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_00281};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00281};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00281};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00281};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00281};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00281};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00281};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00281}; Reference proteome {ECO:0000313|Proteomes:UP000006657}.
FT DOMAIN 107..314
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with beta subunit"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00281"
SQ SEQUENCE 339 AA; 38214 MW; DE192220A9A922F8 CRC64;
MLDKIKQIIS EIGSFTATTP AEVEQFRIKH LSKKGTIAAL FDDFKNVPAD QKKEIGKTLN
ELKTAALDKV NELKEKLCNS DQGKTGVDLT LPGDLIKLGS RHPLSIVKNE ILAIFNKLGF
TISEGPEIED DWHNFSALNF PEEHPARDMQ DTFFIEKNPD IVLHTHTSSV QVRDMETHSL
PIRLVTPGRV FRNEAISARA HCIFHQIEAL YIDENVSFAD LKQTLTYFAK ELFGPETRIR
LRPSYFPFTE PSAEMDVSCS LCHGEGCNVC KGTGWLEILG CGMVDPNVLE LNGIDKEKYT
GFALGMGIER ITMLKYGIKD LRLFFENDIR FLEQFTAAI
//
