AATNT_AQUAE
ID AATNT_AQUAE Reviewed; 824 AA.
AC O66728;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=A-adding tRNA nucleotidyltransferase {ECO:0000305};
DE Short=A-adding TNT {ECO:0000305};
DE EC=2.7.7.- {ECO:0000269|PubMed:11701927};
DE AltName: Full=A-adding enzyme {ECO:0000303|PubMed:11701927};
GN OrderedLocusNames=aq_411 {ECO:0000312|EMBL:AAC06692.1};
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11701927; DOI=10.1126/science.1063816;
RA Tomita K., Weiner A.M.;
RT "Collaboration between CC- and A-adding enzymes to build and repair the 3'-
RT terminal CCA of tRNA in Aquifex aeolicus.";
RL Science 294:1334-1336(2001).
RN [3] {ECO:0007744|PDB:1VFG}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 443-824 IN COMPLEX WITH ATP
RP ANALOG, AND DOMAIN.
RX PubMed=15295603; DOI=10.1038/nature02712;
RA Tomita K., Fukai S., Ishitani R., Ueda T., Takeuchi N., Vassylyev D.G.,
RA Nureki O.;
RT "Structural basis for template-independent RNA polymerization.";
RL Nature 430:700-704(2004).
RN [4] {ECO:0007744|PDB:4WBY, ECO:0007744|PDB:4WBZ, ECO:0007744|PDB:4WC0, ECO:0007744|PDB:4WC1, ECO:0007744|PDB:4WC2, ECO:0007744|PDB:4WC3, ECO:0007744|PDB:4WC4, ECO:0007744|PDB:4WC5, ECO:0007744|PDB:4WC6, ECO:0007744|PDB:4WC7, ECO:0007744|PDB:4X0A}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 428-824 IN COMPLEXES WITH ATP;
RP CTP; TRNA AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DOMAIN.
RX PubMed=25914059; DOI=10.1016/j.str.2015.03.013;
RA Yamashita S., Martinez A., Tomita K.;
RT "Measurement of acceptor-TC helix length of tRNA for terminal A76-addition
RT by A-adding enzyme.";
RL Structure 23:830-842(2015).
CC -!- FUNCTION: tRNA nucleotidyltransferase involved in the synthesis of the
CC tRNA CCA terminus. Adds the terminal adenosine residue to tRNA
CC (PubMed:11701927, PubMed:25914059). Can incorporate CMP into tRNA
CC ending with C74C75 (tRNACC), with very weak efficiency
CC (PubMed:25914059). {ECO:0000269|PubMed:11701927,
CC ECO:0000269|PubMed:25914059}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end +
CC diphosphate; Xref=Rhea:RHEA:60012, Rhea:RHEA-COMP:10468, Rhea:RHEA-
CC COMP:15488, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83069,
CC ChEBI:CHEBI:83071; Evidence={ECO:0000269|PubMed:11701927,
CC ECO:0000269|PubMed:25914059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60013;
CC Evidence={ECO:0000269|PubMed:11701927, ECO:0000269|PubMed:25914059};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:25914059};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=98 uM for ATP {ECO:0000269|PubMed:25914059};
CC KM=220 uM for CTP {ECO:0000269|PubMed:25914059};
CC Note=kcat is 0.10 min(-1) for incorporation of AMP into tRNACC. kcat
CC is 0.00015 min(-1) for incorporation of CMP into tRNACC.
CC {ECO:0000269|PubMed:25914059};
CC -!- DOMAIN: Adopts a seahorse-like shape and consists of four domains:
CC head, neck, body, and tail. {ECO:0000269|PubMed:25914059,
CC ECO:0000305|PubMed:15295603}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
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DR EMBL; AE000657; AAC06692.1; -; Genomic_DNA.
DR PIR; D70337; D70337.
DR RefSeq; NP_213288.1; NC_000918.1.
DR RefSeq; WP_010880226.1; NC_000918.1.
DR PDB; 1VFG; X-ray; 2.80 A; A/B=443-824.
DR PDB; 4WBY; X-ray; 1.50 A; A=428-824.
DR PDB; 4WBZ; X-ray; 3.30 A; A/B=443-824.
DR PDB; 4WC0; X-ray; 3.10 A; A/B=443-824.
DR PDB; 4WC1; X-ray; 3.10 A; A/B=443-824.
DR PDB; 4WC2; X-ray; 2.80 A; A=443-824.
DR PDB; 4WC3; X-ray; 3.10 A; A=443-824.
DR PDB; 4WC4; X-ray; 3.50 A; A=443-824.
DR PDB; 4WC5; X-ray; 3.41 A; A=443-824.
DR PDB; 4WC6; X-ray; 3.41 A; A=443-824.
DR PDB; 4WC7; X-ray; 3.10 A; A=443-824.
DR PDB; 4X0A; X-ray; 3.50 A; A=443-824.
DR PDB; 4X0B; X-ray; 3.20 A; A=443-824.
DR PDBsum; 1VFG; -.
DR PDBsum; 4WBY; -.
DR PDBsum; 4WBZ; -.
DR PDBsum; 4WC0; -.
DR PDBsum; 4WC1; -.
DR PDBsum; 4WC2; -.
DR PDBsum; 4WC3; -.
DR PDBsum; 4WC4; -.
DR PDBsum; 4WC5; -.
DR PDBsum; 4WC6; -.
DR PDBsum; 4WC7; -.
DR PDBsum; 4X0A; -.
DR PDBsum; 4X0B; -.
DR AlphaFoldDB; O66728; -.
DR SMR; O66728; -.
DR STRING; 224324.aq_411; -.
DR EnsemblBacteria; AAC06692; AAC06692; aq_411.
DR KEGG; aae:aq_411; -.
DR PATRIC; fig|224324.8.peg.338; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0617; Bacteria.
DR eggNOG; COG0618; Bacteria.
DR HOGENOM; CLU_015961_5_0_0; -.
DR InParanoid; O66728; -.
DR OMA; ILCHTTA; -.
DR OrthoDB; 2018439at2; -.
DR EvolutionaryTrace; O66728; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.10.580.10; -; 2.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF64182; SSF64182; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; CBS domain; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; Repeat;
KW RNA-binding; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..824
FT /note="A-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000447563"
FT DOMAIN 305..363
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 367..423
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 459..462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25914059,
FT ECO:0000305|PubMed:15295603"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:25914059"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:25914059"
FT BINDING 545..546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25914059,
FT ECO:0000305|PubMed:15295603"
FT BINDING 550
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25914059"
FT BINDING 590..599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25914059"
FT BINDING 603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25914059"
FT BINDING 632
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25914059"
FT HELIX 434..449
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 453..457
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 459..465
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 472..479
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:4WBY"
FT TURN 500..503
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 504..509
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 512..518
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 538..543
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:1VFG"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 570..576
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 586..589
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 592..604
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 610..621
FT /evidence="ECO:0007829|PDB:4WBY"
FT TURN 622..627
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 630..641
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:4WC2"
FT HELIX 646..655
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 659..661
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:4WC3"
FT HELIX 670..689
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 691..693
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 698..705
FT /evidence="ECO:0007829|PDB:4WBY"
FT TURN 706..708
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 711..720
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 725..736
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 738..747
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 751..758
FT /evidence="ECO:0007829|PDB:4WBY"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:4WC0"
FT HELIX 763..769
FT /evidence="ECO:0007829|PDB:4WBY"
FT TURN 773..775
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 776..784
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 786..788
FT /evidence="ECO:0007829|PDB:4WBY"
FT HELIX 793..800
FT /evidence="ECO:0007829|PDB:4WC2"
FT HELIX 807..821
FT /evidence="ECO:0007829|PDB:4WBY"
SQ SEQUENCE 824 AA; 94658 MW; A5B627695C2DAF73 CRC64;
MVCPKVVILS EGADLDSLSA AYGVLKLYPD AYLLKPKHLS KKAGEVFKKY RDKFRVIEDL
PDCFELVLVD THFLPEGLPR ERIKRIIVYD HHPIGDVKEF EGKIEKVGAA TTLVVEEIKE
KGIDINPRDA TLLAFGIYED TGNFTYEGTT PRDALALAFL LEKGANLREI REVVMETYTP
EQIEAVGKIV QSIEKVFING RQISFATAVL ERYQPDINTL LYEIKDLKES DAFFVIIEAE
GKTYVFGRSQ SEDVDVGEIL SHFGGGGHRE AGAVKLENVS AERIKELIKA FLKRKYVKLK
VRDIMNTPPF VLEEHVSVKD ALTELSERGI ANAPVINREG KLVGIISKKA LLKLVKLYPD
EPIELFVNRD FYTLSPDAPV WEAEEILTKF GQKLIPVVED GTVVGVVTRL DILQAVKEDL
EKLKEKRRKI KVPENIEEIA REVGQIAKEM GLRAYIVGGV VRDILLGKEV WDVDFVVEGN
AIELAKELAR RHGVNVHPFP EFGTAHLKIG KLKLEFATAR RETYPRPGAY PKVEPASLKE
DLIRRDFTIN AMAISVNLED YGTLIDYFGG LRDLKDKVIR VLHPVSFIED PVRILRALRF
AGRLNFKLSR STEKLLKQAV NLGLLKEAPR GRLINEIKLA LREDRFLEIL ELYRKYRVLE
EIIEGFQWNE KVLQKLYALR KVVDWHALEF SEERIDYGWL YLLILISNLD YERGKHFLEE
MSAPSWVRET YKFMKFKLGS LKEELKKAKE NYEVYRLLKP LHTSVLLLLM LEEELKEKIK
LYLEKLRKVK LPKEKIEELK KQGLKGKELG ERIEELKREI MNKI
