SYH_BURTA
ID SYH_BURTA Reviewed; 446 AA.
AC Q2SWE3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=BTH_I2235;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00127};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00127}.
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DR EMBL; CP000086; ABC38552.1; -; Genomic_DNA.
DR RefSeq; WP_009890821.1; NZ_CP008785.1.
DR PDB; 4E51; X-ray; 2.65 A; A/B=1-446.
DR PDBsum; 4E51; -.
DR AlphaFoldDB; Q2SWE3; -.
DR SMR; Q2SWE3; -.
DR PRIDE; Q2SWE3; -.
DR EnsemblBacteria; ABC38552; ABC38552; BTH_I2235.
DR KEGG; bte:BTH_I2235; -.
DR HOGENOM; CLU_025113_1_0_4; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 277998at2; -.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 1.
DR CDD; cd00859; HisRS_anticodon; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00127; His_tRNA_synth; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR InterPro; IPR033656; HisRS_anticodon.
DR PANTHER; PTHR43707; PTHR43707; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00442; hisS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..446
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000016329"
FT REGION 403..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 22..41
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4E51"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:4E51"
FT TURN 102..107
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 110..119
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 177..192
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 237..252
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 343..358
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 376..385
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 396..401
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:4E51"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:4E51"
FT HELIX 429..438
FT /evidence="ECO:0007829|PDB:4E51"
SQ SEQUENCE 446 AA; 49588 MW; 4FDB3703EC379690 CRC64;
MTEQKRKLEK LTGVKGMNDI LPQDAGLWEF FEATVKSLLR AYGYQNIRTP IVEHTPLFTR
GIGEVTDIVE KEMYSFVDAL NGENLTLRPE NTAAVVRAAI EHNMLYDGPK RLWYIGPMFR
HERPQRGRYR QFHQVGVEAL GFAGPDADAE IVMMCQRLWE DLGLTGIKLE INSLGLAEER
AAHRVELIKY LEQHADKLDD DAQRRLYTNP LRVLDTKNPA LQEIVRNAPK LIDFLGDVSR
AHFEGLQRLL KANNVPFTIN PRLVRGLDYY NLTVFEWVTD KLGAQGTVAA GGRYDPLIEQ
LGGKPTAACG WAMGIERILE LLKEEHLVPE QEGVDVYVVH QGDAAREQAF IVAERLRDTG
LDVILHCSAD GAGASFKSQM KRADASGAAF AVIFGEDEVT NGTASVKPLR GTGDDGEKSV
QQSVPVESLT EFLINAMVAT AEDGDD
