SYDND_PSEAE
ID SYDND_PSEAE Reviewed; 591 AA.
AC Q51422;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_00044};
DE EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_00044};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
DE Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; OrderedLocusNames=PA0963;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-591.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8982068; DOI=10.1016/s0378-1119(96)00474-x;
RA Hishida T., Iwasaki H., Ishioka K., Shinagawa H.;
RT "Molecular analysis of the Pseudomonas aeruginosa genes, ruvA, ruvB and
RT ruvC, involved in processing of homologous recombination intermediates.";
RL Gene 182:63-70(1996).
RN [3]
RP FUNCTION AS A NON-DISCRIMINATING ASPRS, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND MUTAGENESIS OF HIS-31 AND GLY-82.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16352843; DOI=10.1128/jb.188.1.269-274.2006;
RA Bernard D., Akochy P.M., Beaulieu D., Lapointe J., Roy P.H.;
RT "Two residues in the anticodon recognition domain of the aspartyl-tRNA
RT synthetase from Pseudomonas aeruginosa are individually implicated in the
RT recognition of tRNAAsn.";
RL J. Bacteriol. 188:269-274(2006).
CC -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since
CC it is able to aspartylate not only its cognate tRNA(Asp) but also
CC tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli
CC tRNA(Asp) over tRNA(Asn). Reaction proceeds in two steps: L-aspartate
CC is first activated by ATP to form Asp-AMP and then transferred to the
CC acceptor end of tRNA(Asp/Asn). {ECO:0000269|PubMed:16352843}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asx); Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710,
CC Rhea:RHEA-COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00044, ECO:0000269|PubMed:16352843};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00044}.
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DR EMBL; AE004091; AAG04352.1; -; Genomic_DNA.
DR EMBL; D83138; BAA11815.1; -; Genomic_DNA.
DR PIR; E83524; E83524.
DR PIR; PC4295; PC4295.
DR RefSeq; NP_249654.1; NC_002516.2.
DR RefSeq; WP_003123218.1; NZ_QZGE01000007.1.
DR PDB; 4WJ3; X-ray; 3.70 A; M/N/O/P=1-591.
DR PDB; 4WJ4; X-ray; 3.29 A; A=1-591.
DR PDBsum; 4WJ3; -.
DR PDBsum; 4WJ4; -.
DR AlphaFoldDB; Q51422; -.
DR SMR; Q51422; -.
DR STRING; 287.DR97_974; -.
DR PaxDb; Q51422; -.
DR PRIDE; Q51422; -.
DR EnsemblBacteria; AAG04352; AAG04352; PA0963.
DR GeneID; 881917; -.
DR KEGG; pae:PA0963; -.
DR PATRIC; fig|208964.12.peg.1001; -.
DR PseudoCAP; PA0963; -.
DR HOGENOM; CLU_014330_3_2_6; -.
DR InParanoid; Q51422; -.
DR OMA; YQLDVEM; -.
DR PhylomeDB; Q51422; -.
DR BioCyc; PAER208964:G1FZ6-984-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1360.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR029351; GAD_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
DR Pfam; PF02938; GAD; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55261; SSF55261; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00459; aspS_bact; 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; Reference proteome.
FT CHAIN 1..591
FT /note="Aspartate--tRNA(Asp/Asn) ligase"
FT /id="PRO_0000110924"
FT REGION 198..201
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 174
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 220..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 220
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 450
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 490
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 535..538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 31
FT /note="Important for tRNA non-discrimination"
FT SITE 82
FT /note="Important for tRNA non-discrimination"
FT MUTAGEN 31
FT /note="H->L: Enhances enzyme specificity for tRNA(Asp) over
FT tRNA(Asn) by 3.5-fold, by reducing enzyme's ability to
FT misacylate tRNA(Asn) when tested against E.coli tRNA, but
FT shows little effect when tested against P.aeruginosa tRNA."
FT /evidence="ECO:0000269|PubMed:16352843"
FT MUTAGEN 82
FT /note="G->K: Enhances enzyme specificity for tRNA(Asp) over
FT tRNA(Asn) by 4.2-fold, by reducing enzyme's ability to
FT misacylate tRNA(Asn) when tested against E.coli tRNA, but
FT shows little effect when tested against P.aeruginosa tRNA."
FT /evidence="ECO:0000269|PubMed:16352843"
FT CONFLICT 588
FT /note="P -> A (in Ref. 2; BAA11815)"
FT /evidence="ECO:0000305"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:4WJ4"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 18..30
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4WJ4"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 94..104
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 135..157
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 230..241
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 244..261
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 319..326
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 334..345
FT /evidence="ECO:0007829|PDB:4WJ4"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:4WJ4"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:4WJ4"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 402..419
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 446..450
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 474..479
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 482..490
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 495..503
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 508..513
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 516..523
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 529..535
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 536..544
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:4WJ4"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:4WJ4"
FT TURN 564..567
FT /evidence="ECO:0007829|PDB:4WJ4"
FT HELIX 574..579
FT /evidence="ECO:0007829|PDB:4WJ4"
SQ SEQUENCE 591 AA; 66208 MW; 62B278CA0EDE70A4 CRC64;
MMRSHYCGQL NESLDGQEVT LCGWVHRRRD HGGVIFLDVR DREGLAQVVF DPDRAETFAK
ADRVRSEFVV KITGKVRLRP EGARNPNMAS GSIEVLGYEL EVLNQAETPP FPLDEYSDVG
EETRLRYRFI DLRRPEMAAK LKLRARITSS IRRYLDDNGF LDVETPILGR PTPEGARDYL
VPSRTYPGHF FALPQSPQLF KQLLMVAGFD RYYQIAKCFR DEDLRADRQP EFTQIDIETS
FLDESDIIGI TEKMVRQLFK EVLDVEFDEF PHMPFEEAMR RYGSDKPDLR IPLELVDVAD
QLKEVEFKVF SGPANDPKGR VAALRVPGAA SMPRSQIDDY TKFVGIYGAK GLAYIKVNER
AKGVEGLQSP IVKFIPEANL NVILDRVGAV DGDIVFFGAD KAKIVCDALG ALRIKVGHDL
KLLTREWAPM WVVDFPMFEE NDDGSLSALH HPFTSPKCTP AELEANPGAA LSRAYDMVLN
GTELGGGSIR IHDKSMQQAV FRVLGIDEAE QEEKFGFLLD ALKYGAPPHG GLAFGLDRLV
MLMTGASSIR EVIAFPKTQS AGDVMTQAPG SVDGKALREL HIRLREQPKA E
