ID A0A174BYN6_9BACE Unreviewed; 1162 AA.
AC A0A174BYN6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02003};
DE EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02003};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003};
DE Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02003};
GN Name=ileS {ECO:0000256|HAMAP-Rule:MF_02003,
GN ECO:0000313|EMBL:CUO06351.1};
GN ORFNames=ERS852397_01283 {ECO:0000313|EMBL:CUO06351.1}, F2Z22_20010
GN {ECO:0000313|EMBL:KAA5227131.1};
OS Bacteroides finegoldii.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=338188 {ECO:0000313|EMBL:CUO06351.1, ECO:0000313|Proteomes:UP000095517};
RN [1] {ECO:0000313|EMBL:CUO06351.1, ECO:0000313|Proteomes:UP000095517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608840 {ECO:0000313|EMBL:CUO06351.1,
RC ECO:0000313|Proteomes:UP000095517};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA5227131.1, ECO:0000313|Proteomes:UP000421791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A6 {ECO:0000313|EMBL:KAA5227131.1,
RC ECO:0000313|Proteomes:UP000421791};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
CC -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS
CC can inadvertently accommodate and process structurally similar amino
CC acids such as valine, to avoid such errors it has two additional
CC distinct tRNA(Ile)-dependent editing activities. One activity is
CC designated as 'pretransfer' editing and involves the hydrolysis of
CC activated Val-AMP. The other activity is designated 'posttransfer'
CC editing and involves deacylation of mischarged Val-tRNA(Ile).
CC {ECO:0000256|ARBA:ARBA00025217, ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC ChEBI:CHEBI:456215; EC=6.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000114, ECO:0000256|HAMAP-
CC Rule:MF_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and
CC one for editing. The misactivated valine is translocated from the
CC active site to the editing site, which sterically excludes the
CC correctly activated isoleucine. The single editing site contains two
CC valyl binding pockets, one specific for each substrate (Val-AMP or Val-
CC tRNA(Ile)). {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02003}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CYZH01000006; CUO06351.1; -; Genomic_DNA.
DR EMBL; VWAK01000052; KAA5227131.1; -; Genomic_DNA.
DR RefSeq; WP_007748413.1; NZ_VWAO01000050.1.
DR AlphaFoldDB; A0A174BYN6; -.
DR STRING; 338188.ERS852397_01283; -.
DR GeneID; 61624290; -.
DR Proteomes; UP000095517; Unassembled WGS sequence.
DR Proteomes; UP000421791; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 3.30.720.200; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033709; Anticodon_Ile_ABEc.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023586; Ile-tRNA-ligase_type2.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR00392; ileS; 1.
DR PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF19302; DUF5915; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02003};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02003}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02003};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02003};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02003}; Reference proteome {ECO:0000313|Proteomes:UP000095517};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 20..749
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 797..948
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 710..714
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 713
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1162 AA; 132866 MW; 82849EA7AE7A6C93 CRC64;
MGKRFTEYSQ FDLSQVNKDV LKKWDENQVF AKSMTERDGC PSFVFFEGPP SANGMPGIHH
VMARTIKDIF CRYKTMKGYQ VKRKAGWDTH GLPVELGVEK ALGITKEDIG KKISVAEYNA
ACRKDVMKFT KEWEDLTHKM GYWVDMKHPY ITYDNRYIET LWWLLKQLYK KGLLYKGYTI
QPYSPAAGTG LSSHELNQPG CYRDVKDTTM VAQFKIKNPK PEMTGWGTPY FLAWTTTPWT
LPSNTALCVG PKFDYVVVQS YNTYNGEPIT VVLAKALLNT HFNPKAADLN LEDYKPGDKL
VPFKVVAEYK GTELVGMEYE QLIPWVKPIE VSEDGMWKVS DKGFRVIQGD YVTTEDGTGI
VHIAPTFGAD DANVARAAGI PSLFMINKKG ETRPMVDLTG KFYLLDELDE RFVKECVDVD
KYKEYQGAWV KNAYDPQFTV DGKYDEKAAQ AAESLDIALC MMMKAGKQAF KIEKHVHNYP
HCWRTDKPVL YYPLDSWFIR STACKERMME LNKTINWKPE STGTGRFGKW LENLNDWNLS
RSRYWGTPLP IWRTEDNTDE KCIESVEELY NEIEKSVAAG FMQSNPYKDK GFVPGEYTEQ
NYDKIDLHRP YVDDIILVSK DGKPMKREMD LIDVWFDSGS MPYAQIHYPF ENKELLDSRQ
VYPADFIAEG VDQTRGWFFT LHAIATMVFD SVSYKAVISN GLVLDKNGNK MSKRLGNAVD
PFSTIEKYGS DPLRWYMITN SSPWDNLKFD VDGIEEVRRK FFGTLYNTYS FFVLYANVDG
FEYKEADVPM AERPEIDRWI LSVLNTLIKE VDTCYNEYEP TKAGRLISDF VNDNLSNWYV
RLNRKRFWGG EFTQDKLSAY QTLYICLETV AKLMSPIAPF YADRLYTDLI TATGRDNVVS
VHLAKFPEYQ ENSIDKELEA RMKMAQDVTS MVLALRRKVN IKVRQPLQCI MVPVVDEEQK
AHIEAVKNLI MNEVNVKEVK FVDGAAGVLV KKVKCDFKKL GPKFGKQMKA VAAAVAGMSQ
EAIAELEKNG KYVLNLDGAE AVIEAADVEI FSEDIPGWLV ANEGKLTVAL EVTVTEELRR
EGIARELVNR IQNIRKSSGF EITDKIKITI SKNTQTDDAV KEYNTYICNQ VLGTSLGLVD
EVKDGIELNF DDFSLFVNVI KD
//
