SYDND_MYCTU
ID SYDND_MYCTU Reviewed; 594 AA.
AC P9WFW3; L0TCT5; Q50649;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
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=Rv2572c;
GN ORFNames=MTCY227.29;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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). Reaction proceeds in two steps: L-aspartate is first
CC activated by ATP to form Asp-AMP and then transferred to the acceptor
CC end of tRNA(Asp/Asn). {ECO:0000255|HAMAP-Rule:MF_00044}.
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};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP45368.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL123456; CCP45368.1; ALT_INIT; Genomic_DNA.
DR PIR; C70724; C70724.
DR RefSeq; NP_217088.1; NC_000962.3.
DR PDB; 5W25; X-ray; 2.65 A; A/B=2-594.
DR PDBsum; 5W25; -.
DR AlphaFoldDB; P9WFW3; -.
DR SMR; P9WFW3; -.
DR STRING; 83332.Rv2572c; -.
DR ChEMBL; CHEMBL4662921; -.
DR PaxDb; P9WFW3; -.
DR DNASU; 888532; -.
DR GeneID; 888532; -.
DR KEGG; mtu:Rv2572c; -.
DR TubercuList; Rv2572c; -.
DR eggNOG; COG0173; Bacteria.
DR OMA; YQLDVEM; -.
DR BRENDA; 6.1.1.12; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
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..594
FT /note="Aspartate--tRNA(Asp/Asn) ligase"
FT /id="PRO_0000110908"
FT REGION 197..200
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT REGION 566..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 173
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 219..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 219
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 451
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 492
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 537..540
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 /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 83
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 18..31
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 134..156
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 229..240
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 243..258
FT /evidence="ECO:0007829|PDB:5W25"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:5W25"
FT TURN 298..301
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 327..338
FT /evidence="ECO:0007829|PDB:5W25"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 367..375
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 391..408
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 431..436
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 442..451
FT /evidence="ECO:0007829|PDB:5W25"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 473..481
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 484..492
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 496..505
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 510..523
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 531..537
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 538..546
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 551..554
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:5W25"
FT TURN 566..569
FT /evidence="ECO:0007829|PDB:5W25"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:5W25"
FT HELIX 576..580
FT /evidence="ECO:0007829|PDB:5W25"
SQ SEQUENCE 594 AA; 64981 MW; D0013840069FE283 CRC64;
MLRSHAAGLL REGDAGQQVT LAGWVARRRD HGGVIFIDLR DASGIAQVVF RDPQDTEVLA
QAHRLRAEFC VSVAGVVEIR PEGNANPEIA TGEIEVNATS LTVLGECAPL PFQLDEPAGE
ELRLKYRYLD LRRDDPAAAI RLRSRVNAAA RAVLARHDFV EIETPTITRS TPEGARDFLV
PARLHPGSFY ALPQSPQLFK QLLMVAGMER YYQIARCYRD EDFRADRQPE FTQLDMEMSF
VDAEDIIAIS EEVLTELWAL IGYRIPTPIP RIGYAEAMRR FGTDKPDLRF GLELVECTDF
FSDTTFRVFQ APYVGAVVMP GGASQPRRTL DGWQDWAKQR GHRGLAYVLV AEDGTLGGPV
AKNLTEAERT GLADHVGAKP GDCIFFSAGP VKSSRALLGA ARVEIANRLG LIDPDAWAFV
WVVDPPLFEP ADEATAAGEV AVGSGAWTAV HHAFTAPKPE WEDRIESDTG SVLADAYDIV
CNGHEIGGGS VRIHRRDIQE RVFAVMGLDK AEAEEKFGFL LEAFMFGAPP HGGIAFGWDR
TTALLAGMDS IREVIAFPKT GGGVDPLTDA PAPITAQQRK ESGIDAQPKR VQQA
