ID   SYI_PORGI               Reviewed;        1137 AA.
AC   Q7MUD3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003};
GN   Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003};
GN   OrderedLocusNames=PG_1596;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR   EMBL; AE015924; AAQ66625.1; -; Genomic_DNA.
DR   RefSeq; WP_005874631.1; NC_002950.2.
DR   AlphaFoldDB; Q7MUD3; -.
DR   SMR; Q7MUD3; -.
DR   STRING; 242619.PG_1596; -.
DR   EnsemblBacteria; AAQ66625; AAQ66625; PG_1596.
DR   KEGG; pgi:PG_1596; -.
DR   PATRIC; fig|242619.8.peg.1479; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_10; -.
DR   BioCyc; PGIN242619:G1G02-1490-MONOMER; -.
DR   Proteomes; UP000000588; 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   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; 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; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..1137
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098554"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT   MOTIF           688..692
FT                   /note="'KMSKS' region"
FT   BINDING         691
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1137 AA;  129945 MW;  2952F7799895B543 CRC64;
     MSRRFAEYES LDLSRVNEEV LADWMQHRLF EESLKSREGA PSFVFYEGPP SANGMPGIHH
     VMARAIKDTI CRYKTMKGFR VDRKAGWDTH GLPVELGVEK SLGITKEDIG KSISVEEYNA
     ACRRDVMKFT KEWEDLTHKM GYWVDMEHPY ITYDNRYIET LWWLLAELYK KGLLYKGYTI
     QPYSPAAGTG LSTHELNQPG CYRDVKDTTC VAQFKIMDPK PEMQLHGDAF FLAWTTTPWT
     LPSNTALCVG PEIEYLAVQT FNPYNGIPIT VVLGKPLLHT LFNPKGECEE IPASYDPAQK
     LLPYKVIASW KGKELEGMRY EQLIPWVNPG EGAFRVITGD FVTTEDGTGI VHIAPTFGAD
     DDRVAKKSGV PPLMLRDKEG NMRPMVDLAG RYFPTTDLDP VFVEKHMDLP LYDVYAGRYV
     KNAYDAGKTE KDETLDVELC VMLKMQNRVF RIEKMTHNYP HCWRTDKPVL YYPLDSWFIR
     TTACKEEMIA NNGKIYWKPE STGTGRFGKW LENLQDWNLS RSRYWGTPLP IWRTEDGSEE
     ICIGSVEELY NEIEKAVKAG MMERNPWAGF KPGVYTEENY AKIDLHRPFV DGITLCSPSG
     QPMRRELDLI DVWFDSGAMP YAQMHYPFEN RERVEDGSVF PADFIAEGVD QTRGWFFTLH
     AIATMISGTS SFKVVVSNGL VLDKKGNKMS KRLGNAVDPF ETIKKYGSDP LRWYMITNSS
     PWDNLKFDTD GVEEVRRKFF GTLYNTYQFF ALYANLDGFT GEEESIPFAK RPEIDRWILS
     ELNTLIREVD DQLSDYEPTR AGRAISDFVS ENLSNWYVRL SRRRFWAGDM TEDKLSAYQT
     LYTSLLTVSK LMAPISPFYA DRLYRDLTGK DESVHLALFP RPDQSQVDRA LEQSMQMAQQ
     ISSMVLALRR RVNLKVRQPL ATLMIPAIDD EQRRCIESVQ PLILSEVNVK ELRFVDDSMG
     ILVKRIKPDF KRLGPRYGKV MKALAEAVTA MTQEEIRSLE KAGTFRMEVA GTPVELELAD
     VEIVSEDIPG WLVANEGNLT VALDITVTDE LRSEGLAREL VNRVQNIRKQ SGFEVSDKVD
     VLLLSNDIMD KVVAEHHDYI AQQIQAESLE ISDAVSDGVE LDFDDFVLSI QVVKHQG
//