ID C1A881_GEMAT Unreviewed; 1097 AA.
AC C1A881;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
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:BAH38441.1};
GN OrderedLocusNames=GAU_1399 {ECO:0000313|EMBL:BAH38441.1};
OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS 100505).
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH38441.1, ECO:0000313|Proteomes:UP000002209};
RN [1] {ECO:0000313|Proteomes:UP000002209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC {ECO:0000313|Proteomes:UP000002209};
RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT novel phylum Gemmatimonadetes.";
RL Submitted (MAR-2006) 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}.
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DR EMBL; AP009153; BAH38441.1; -; Genomic_DNA.
DR RefSeq; WP_012682888.1; NC_012489.1.
DR AlphaFoldDB; C1A881; -.
DR STRING; 379066.GAU_1399; -.
DR KEGG; gau:GAU_1399; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_0; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000002209; Chromosome.
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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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:UP000002209};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 25..672
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 727..870
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 55..65
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 640..644
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 643
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1097 AA; 121756 MW; B41AA18192BD174E CRC64;
MTVPQDAVLF PLLPETSADA LETELLATWE SEQLFEQTQD ARANGKPFVF FEGPPTANGR
PGIHHVFSRT IKDLFCRHRA MQGHFVPRKA GWDTHGLPVE IEVEKELQRE EAARQGVDPS
EIAKLGGKQL IEQVGVAEFN RRCRESVWKY RGEWEKLSQR TAYWLDYGDP YVTYSHNFVE
SAWWALRTLH DKQLLTRGHK ILPYCARCGT ALSSHEVAQG YEDVEDPSVY IALDLLDEHG
NAPAMRRRVL VWTTTPWTLV SNTALAVHPD LSYVELRKKT GAEWTIILAE ARAAGVLGAD
WTDRWDVVGT MTGRDLMGRR YRRPLDWVPF PDEGEHEIIV GEDFVSADDG SGVVHMAPAF
GADDYAAGQR NGLAFLQPVN ARGEFVDGVP EVAGVFVKKA DARILEVLKE RDVLWKASTF
VHSYPHCWRC GTPLLYYARG SWFVRTTAVR DQLLARNGRV NWNPPEVGSG RFGEWLSNNV
DWAISRDRYW GTPLPVWIND EDPTEVDVIG SYADLAQRIG RALPDDFDPH KPHIDQYTWP
APSGKGTMRR VPEVIDTWFD SGAMPFAQWH YPFENADKVQ AQYPADYICE GVDQTRGWFY
SLLAIATTLG DALPNNGDDM AAPYRNVVVN DLVLDASGQK MSKSRGNVVN PWEVLERHGA
DAVRLFLVGS SQVWVPRRFD ENAIRETAGR FLLTVRNVYN GIFAQYANFG WTPSAADPQI
ADRPALDRWI LSRLSRVEQE ANQHLNNYDA TLAARRVMQF MDDDVSKWYV RQSRARFYDV
EGADNRAAFA TLHEVLTVTC RLLAPFAPFM TDALHRALTG TSVHLASYTR ESPTPVDETL
EAAMQDLRTL TGLAHAARDV ADVKVRQPLP SLQCVVPGDA DAVSALAGLL AAELNVKQVE
FVTSTDALVS LEAKANFRTL GKKFGKETPL VAEAVGTMPA DLLRQLAAGE SVSIDVAGAA
RLIAPDDVAI IRRASGDAVV QEHAGYGVAL DATITPALRA EGLAREVVSR VQRLRKEAQL
AVSDRITVAV AGDEELQGAV AAHRDHIAQE VLAVRLLLGD EAGSPFRTDG NDSTWTASLT
VDVDGRPVRL ALTKEGS
//
