MIAA_ALKHC
ID MIAA_ALKHC Reviewed; 314 AA.
AC Q9KAC3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=BH2366;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of the full-length tRNA isopentenylpyrophosphate
RT transferase (BH2366) from Bacillus halodurans, northeast structural
RT genomics consortium target BHR41.";
RL Submitted (FEB-2009) to the PDB data bank.
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). {ECO:0000250}.
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; BA000004; BAB06085.1; -; Genomic_DNA.
DR PIR; F83945; F83945.
DR PDB; 2QGN; X-ray; 2.40 A; A=1-314.
DR PDB; 3EXA; X-ray; 2.30 A; A/B/C/D=1-314.
DR PDBsum; 2QGN; -.
DR PDBsum; 3EXA; -.
DR AlphaFoldDB; Q9KAC3; -.
DR SMR; Q9KAC3; -.
DR STRING; 272558.10174986; -.
DR DNASU; 891429; -.
DR EnsemblBacteria; BAB06085; BAB06085; BAB06085.
DR KEGG; bha:BH2366; -.
DR eggNOG; COG0324; Bacteria.
DR HOGENOM; CLU_032616_0_1_9; -.
DR OMA; YAKRQYT; -.
DR OrthoDB; 1069591at2; -.
DR EvolutionaryTrace; Q9KAC3; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
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; 2.
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..314
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_0000163873"
FT REGION 35..38
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 160..164
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 239..244
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 272..279
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 12..17
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 101
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT SITE 124
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:3EXA"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3EXA"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:3EXA"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:3EXA"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 74..90
FT /evidence="ECO:0007829|PDB:3EXA"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:3EXA"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:3EXA"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:2QGN"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 256..279
FT /evidence="ECO:0007829|PDB:3EXA"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:2QGN"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:3EXA"
FT HELIX 294..314
FT /evidence="ECO:0007829|PDB:3EXA"
SQ SEQUENCE 314 AA; 35763 MW; E1027425C1524942 CRC64;
MKEKLVAIVG PTAVGKTKTS VMLAKRLNGE VISGDSMQVY RGMDIGTAKI TAEEMDGVPH
HLIDIKDPSE SFSVADFQDL ATPLITEIHE RGRLPFLVGG TGLYVNAVIH QFNLGDIRAD
EDYRHELEAF VNSYGVQALH DKLSKIDPKA AAAIHPNNYR RVIRALEIIK LTGKTVTEQA
RHEEETPSPY NLVMIGLTME RDVLYDRINR RVDQMVEEGL IDEAKKLYDR GIRDCQSVQA
IGYKEMYDYL DGNVTLEEAI DTLKRNSRRY AKRQLTWFRN KANVTWFDMT DVDFDKKIME
IHNFIAGKLE EKSK
