MIAA_PSEAE
ID MIAA_PSEAE Reviewed; 323 AA.
AC Q9HUL9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=tRNA dimethylallyltransferase;
DE EC=2.5.1.75;
DE AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase;
DE Short=DMAPP:tRNA dimethylallyltransferase;
DE Short=DMATase;
DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase;
DE Short=IPP transferase;
DE Short=IPPT;
DE Short=IPTase;
GN Name=miaA; OrderedLocusNames=PA4945;
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 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PYROPHOSPHATE.
RX PubMed=17292915; DOI=10.1016/j.jmb.2007.01.048;
RA Xie W., Zhou C., Huang R.H.;
RT "Structure of tRNA dimethylallyltransferase: RNA modification through a
RT channel.";
RL J. Mol. Biol. 367:872-881(2007).
CC -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the
CC adenine at position 37 in tRNAs that read codons beginning with
CC uridine, leading to the formation of N6-(dimethylallyl)adenosine
CC (i(6)A).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate =
CC diphosphate + N(6)-dimethylallyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74415; EC=2.5.1.75;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08330.1; -; Genomic_DNA.
DR PIR; E83028; E83028.
DR RefSeq; NP_253632.1; NC_002516.2.
DR RefSeq; WP_003113929.1; NZ_QZGE01000002.1.
DR PDB; 3CRM; X-ray; 1.90 A; A=1-323.
DR PDB; 3CRQ; X-ray; 2.20 A; A=1-323.
DR PDB; 3CRR; X-ray; 1.90 A; A=1-323.
DR PDBsum; 3CRM; -.
DR PDBsum; 3CRQ; -.
DR PDBsum; 3CRR; -.
DR AlphaFoldDB; Q9HUL9; -.
DR SMR; Q9HUL9; -.
DR STRING; 287.DR97_2298; -.
DR PaxDb; Q9HUL9; -.
DR PRIDE; Q9HUL9; -.
DR DNASU; 878016; -.
DR EnsemblBacteria; AAG08330; AAG08330; PA4945.
DR GeneID; 878016; -.
DR KEGG; pae:PA4945; -.
DR PATRIC; fig|208964.12.peg.5178; -.
DR PseudoCAP; PA4945; -.
DR HOGENOM; CLU_032616_0_0_6; -.
DR InParanoid; Q9HUL9; -.
DR OMA; YAKRQYT; -.
DR PhylomeDB; Q9HUL9; -.
DR BioCyc; PAER208964:G1FZ6-5061-MON; -.
DR EvolutionaryTrace; Q9HUL9; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00185; IPP_trans; 1.
DR InterPro; IPR039657; Dimethylallyltransferase.
DR InterPro; IPR018022; IPT.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11088; PTHR11088; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00174; miaA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Magnesium; Nucleotide-binding;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..323
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_0000163956"
FT REGION 37..40
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 161..165
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 253..258
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 286..293
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 14..19
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 103
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT SITE 125
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:3CRM"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:3CRM"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3CRM"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:3CRM"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:3CRM"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:3CRM"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3CRQ"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:3CRM"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:3CRM"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:3CRM"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:3CRM"
FT HELIX 213..229
FT /evidence="ECO:0007829|PDB:3CRM"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:3CRM"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3CRM"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:3CRM"
FT HELIX 270..293
FT /evidence="ECO:0007829|PDB:3CRM"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:3CRM"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:3CRM"
SQ SEQUENCE 323 AA; 35769 MW; B33DFB9EA45157CF CRC64;
MSSLPPAIFL MGPTAAGKTD LAMALADALP CELISVDSAL IYRGMDIGTA KPSRELLARY
PHRLIDIRDP AESYSAAEFR ADALAAMAKA TARGRIPLLV GGTMLYYKAL LEGLADMPGA
DPEVRAAIEA EAQAEGWEAL HRQLAEVDPE SAARIHPNDP QRLMRALEVY RLGGVSMSDL
RRRQSAEKAD FDASGRNQLP YTVAQLAIAP EQRQVLHARI AQRFRQMLEQ GFIAEVEALH
ARSDLHAGLP SIRAVGYRQV WDYLDGKLSY AEMTERGIIA TRQLAKRQFT WLRSWSHLHW
MDSLAGDNLP RALKYLKTVS ILA