ID A0A0C1I6F9_9BACT Unreviewed; 1136 AA.
AC A0A0C1I6F9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 ORFNames=HY58_14845 {ECO:0000313|EMBL:KIC89650.1};
OS Flavihumibacter sp. ZG627.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1463156 {ECO:0000313|EMBL:KIC89650.1, ECO:0000313|Proteomes:UP000031400};
RN [1] {ECO:0000313|EMBL:KIC89650.1, ECO:0000313|Proteomes:UP000031400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZG627 {ECO:0000313|EMBL:KIC89650.1,
RC ECO:0000313|Proteomes:UP000031400};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter carbonis ZG627.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KIC89650.1}.
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; JPHF01000008; KIC89650.1; -; Genomic_DNA.
DR RefSeq; WP_039133445.1; NZ_JPHF01000008.1.
DR AlphaFoldDB; A0A0C1I6F9; -.
DR STRING; 1463156.HY58_14845; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000031400; 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 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:UP000031400};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 20..716
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 767..919
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 680..684
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1136 AA; 129721 MW; 5CB6E3D021977233 CRC64;
MAAKYREYQQ LNLPSIESEI LGKWTEHQAF EKSVSLREGK EPFVFYEGPP SANGMPGIHH
VISRTLKDLV CRYKTMQGYQ VKRKGGWDTH GLPIELGVEK ELGITKEDIG KSISVEEYNQ
KCRDAVLRFK DKWDDLTRKM GYWVDLNDPY ITFENNYIET LWWLLKRLHS KGLLYKSVSI
QPYSPAAGTG LSSHELNQPG TYKDVKDTSV VAMFKALRDE RSEFLFDAAS EVINPNLYAA
SIIETTEIFF LAWTTTPWTL PSNLGLTVGP NIDYVLIKTF NPYTHLPIHV VLAKSLLGKY
FKPEGENGDF DGYGPDTKLL PWRQLNEFKG KVLEHCRYEQ LLPYEANSAD VAGGDPFRVL
LDTFVTTEDG TGIVHTAPAF GADDYKVGKK YGIGILTMVD REGKFVEGLG EFSNRYVKNY
KDEPDYVDVN IDISVKLKKE NRAFKVEKYE HSYPHCWRTD KPVLYYPLDA WFIKTTAIKD
RMVELNKTIN WKPKATGEGR FGNWLENMVD WNLSRSRYWG TPLPIWRTED GKEEKCIGSI
EELKMEIIKA REVLGGEVNK NYLHDNELDL HKPYVDEVVL VSDTGKVMRR EPDLIDVWFD
SGAMPYAQWG LDQLKVRAGD ETPFNAPFGQ NFPADFICEG VDQTRGWFYT LHALAALLYD
SVAYKTVVSN GLVLDKNGNK MSKRLGNVVD PFSTIENFGA DATRWYLITN ASPWDSLKFD
LEGIREVQRK FFGTLYNTYQ FFVLYANVDG FSFNEKYVPL EDRPEIDRWI LSSLNSLVRD
VTAALNDYEP TQAGRLVEDF VDEHLSNWYV RLCRRRFWKG EYSTDKIAAY QTLYECLETI
SRLIAPVSPF FADWLFTNLN TVTGRFKEGS VHHTDYPVSD AGLIDTALEE RMQLAQDSSS
LVLSLRKKVN IKVRQPLQRI LIPVLNPSMK DQLEKVADLI RSEVNVKEIQ YLTDADGFIK
KKIKPNFQAL GKRLGSKMKA VTAAIGALDQ EAISLLEKEG SYSLEIDSEP LILQIHEVEI
TSEDIPGWMV SSKGALTVAL DVTVTPELEQ EGNARELVNR IQKIRKDNGY ELTDRILVKL
SQAGVLAESI RHFGPYIKEE VLADELEMVE ELGNGMAIEV NDQPVRVWVD KVTRTQ
//
