SYH_PSEU2
ID SYH_PSEU2 Reviewed; 429 AA.
AC Q4ZX22;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=Psyr_1249;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(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; CP000075; AAY36300.1; -; Genomic_DNA.
DR RefSeq; WP_011266910.1; NC_007005.1.
DR RefSeq; YP_234338.1; NC_007005.1.
DR AlphaFoldDB; Q4ZX22; -.
DR SMR; Q4ZX22; -.
DR STRING; 205918.Psyr_1249; -.
DR EnsemblBacteria; AAY36300; AAY36300; Psyr_1249.
DR KEGG; psb:Psyr_1249; -.
DR PATRIC; fig|205918.7.peg.1281; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_6; -.
DR OMA; CDFDFIG; -.
DR Proteomes; UP000000426; Chromosome.
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 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 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..429
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136229"
SQ SEQUENCE 429 AA; 47829 MW; 6E7848DAC86E62D9 CRC64;
MSKSLQAIRG MNDILPEQTP LWRHFEGTVA RLLDNYGYRQ IRMPIVEFTE LFKRSIGEVT
DIVEKEMYTF ADRNGDSLTL RPEGTAACVR AVLEHGITGG GQVQKLWYIG PMFRHERPQK
GRYRQFHQIG VEVFNLDGPD IDAELIVMTW RLWGLLGIRD AVKLELNSLG TSEARARYRE
ALVEYLSARL DQLDEDSQRR LKTNPLRVLD TKHPETQAVL VDAPKLADYL DDESRVHFEG
LKARLDAAGI PYVINPKLVR GLDYYSKTVF EWVTDQLGAQ GTVCAGGRYD GLVEQMGGKP
TAGVGFAMGI ERLVLLLETL EQVPEEIARQ VDVYLCAFGE AAELAALALT EKVRDQLPTL
RLQVNAGAGS FKSQFKKADK SGALYALILG EEELAAKVIG VKPLRGQGEQ QNIAWDALSE
HLASCVVQG