SYH_ACIBS
ID SYH_ACIBS Reviewed; 430 AA.
AC B0VKR7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=ABSDF3000;
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU468230; CAP02286.1; -; Genomic_DNA.
DR PDB; 5E3I; X-ray; 2.20 A; A/B=1-430.
DR PDBsum; 5E3I; -.
DR AlphaFoldDB; B0VKR7; -.
DR SMR; B0VKR7; -.
DR EnsemblBacteria; CAP02286; CAP02286; ABSDF3000.
DR KEGG; abm:ABSDF3000; -.
DR HOGENOM; CLU_025113_1_0_6; -.
DR OMA; CDFDFIG; -.
DR Proteomes; UP000001741; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..430
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000095523"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:5E3I"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 124..135
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 139..155
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 232..247
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:5E3I"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 343..359
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 394..399
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:5E3I"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:5E3I"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:5E3I"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:5E3I"
SQ SEQUENCE 430 AA; 48434 MW; EA14E0A8A7AC9CF6 CRC64;
MSSIVAIKGF NDVLPTQTAA WRRLEQHLAS LMDAYGYQQI RLPIVEQTGL FKRAIGDATD
IVEKEMYTFF DKGNPPESLT LRPEGTAGCV RALVEHNLLR GATPRVWYMG PMFRYEKPQK
GRYRQFHQFG VETFGVATPD IDAELIMLTA RLWKRMGVDH MVQLELNTLG ETDERTEYRN
ALVAFLNEHK DALDEDSQRR LTTNPLRILD SKIESTQKIL ENAPKLHDFL KEDSLSHFQQ
LQDYLTAAGI KFVINQKLVR GLDYYNKTVF EWTTTALGSQ GTVCAGGRYD GLVGQLKGKA
DQSVPAVGFA MGMERLLLLL EQVEQAEIVR HCEAFLVAEP AYQSKALVLA EQLRDQLEAA
NSNIRIKTGS QSSMKSQMKK ADQAGAVYAI ILGEREWEAQ QLAVKELATA EQSQVALAEL
VPFLIEKFTK
