ID E4VC62_BIFBI Unreviewed; 1107 AA.
AC E4VC62;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
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:EFR51177.1};
GN ORFNames=BBNG_01725 {ECO:0000313|EMBL:EFR51177.1};
OS Bifidobacterium bifidum NCIMB 41171.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=398513 {ECO:0000313|EMBL:EFR51177.1, ECO:0000313|Proteomes:UP000002776};
RN [1] {ECO:0000313|EMBL:EFR51177.1, ECO:0000313|Proteomes:UP000002776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 41171 {ECO:0000313|EMBL:EFR51177.1,
RC ECO:0000313|Proteomes:UP000002776};
RG The Broad Institute Genome Sequencing Platform;
RA Goulas T., Tzortzis G., Gibson G.R., Ward D., Mehta T., Young S., Jaffe D.,
RA Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., Sykes S.,
RA Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J., Nusbaum C.,
RA Birren B.;
RT "Annotation of Bifidobacterium bifidum strain NCIMB 41171.";
RL Submitted (AUG-2008) 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|ARBA:ARBA00007078,
CC ECO:0000256|HAMAP-Rule:MF_02003}.
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DR EMBL; DS990230; EFR51177.1; -; Genomic_DNA.
DR AlphaFoldDB; E4VC62; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_11; -.
DR Proteomes; UP000002776; 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; 3.40.50.620; 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; IPR001412; aa-tRNA-synth_I_CS.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}; Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 35..687
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 746..897
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 69..79
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 653..657
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1107 AA; 124856 MW; C04BCFE6EC5A6405 CRC64;
MSETTNSHVY PKANEGGETA SVAPNPSFPN MEETVLKYWD KDDTFNKSVE RNPSGDHSQN
EFVFFDGPPF ANGLPHYGHL LTGYAKDVIP RYQTMKGRKV NRVFGWDTHG LPAELEAQKE
LGIDSVDQIE KMGIDKFNDA CRASVLKYTH EWQDYVHRQA RWVDFEHGYK TLNIPYMESV
MWAFKQLYEK GLAYQGYRVL PYCPKDQTPL SAHELRMDAD VYQDRQDTTV SVAVKLRDEE
DAYAVFWTTT PWTVPTNFAI VVGADIDYVE VRPTQGKYAG KKFYFGKPLL SKYEKELGED
YEVVRELKGS EMAGWRYWPV FPYFAGDKAE SEGNVPGPEG YQIFTADYVD TVEGTGLVHQ
APYGEDDMNT LNAHGIKSTD VLDAGCRFTA QCPDYEGMYV FDANKPILRN LRNGDGPLAE
IPAEHRAILF QEKSYVHSYP HCWRCATPLI YKPVSSWFVS VTKIKPRLLE LNQQINWIPE
NVKDGQFGKW LANARDWSIS RNRFWGSPIP VWVSDDPKYP RVDVYGSLEE LKADFGDYPR
DKDGNVNMHR PWIDNLTRVN PDDPTGKSHM HRISDVLDCW FESGSMSFAQ FHYPFENKEK
FEQHFPADYI VEYIGQTRGW FYLLHVMATA LFDRPAFKNV ICHGIVLGSD GQKMSKHLRN
YPDVNGVFDK YGSDAMRWFL MSSPILRGGN LIVTAEGIRD TVRQVMLPVW SSYYFFTLYA
NAANGGAGFD ARQLHADEVA GLPEMDRYLL ARTRRLVERV EKSLDEFAIS DACDAASDFI
DVLTNWYIRN TRDRFWKEDT NAFNTLYTVL EVFMRVLAPL APMESESVWR GLTGGESVHL
ADWPYVSDEK TGEATELGRV LVDDPALVDA MEKVREIVSG TLSLRKAAQI RVRQPLAKLT
VVVEDVDAVK AYDEILKSEL NIKDIEFCTM EDAGSQGLKI VHELKVNARA AGPRLGKQVQ
FAIKASKTGA WHVDAATGAP VVETPNGEVA LEAGEYELIN RVEEENAAEV DASVSAALPT
GGFVILDTVL TADLEAEGYA RDVIRAVQDA RKAADLDIAD RIALVLTVPS ANVADVERFR
DLIAHETLAT SFAVKEGAEL GVEVAKA
//
