MIAA_STAES
ID MIAA_STAES Reviewed; 332 AA.
AC Q8CQL3;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=SE_0981;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of tRNA delta(2)-isopentenylpyrophosphate transferase
RT (SE0981) from Staphylococcus epidermidis.";
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; AE015929; AAO04578.1; -; Genomic_DNA.
DR RefSeq; NP_764536.1; NC_004461.1.
DR RefSeq; WP_002439583.1; NZ_WBME01000001.1.
DR PDB; 3D3Q; X-ray; 2.70 A; A/B=1-332.
DR PDBsum; 3D3Q; -.
DR AlphaFoldDB; Q8CQL3; -.
DR SMR; Q8CQL3; -.
DR STRING; 176280.SE_0981; -.
DR PRIDE; Q8CQL3; -.
DR EnsemblBacteria; AAO04578; AAO04578; SE_0981.
DR GeneID; 50018885; -.
DR KEGG; sep:SE_0981; -.
DR PATRIC; fig|176280.10.peg.955; -.
DR eggNOG; COG0324; Bacteria.
DR HOGENOM; CLU_032616_0_1_9; -.
DR OMA; YAKRQYT; -.
DR EvolutionaryTrace; Q8CQL3; -.
DR Proteomes; UP000001411; 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; Transferase;
KW tRNA processing.
FT CHAIN 1..332
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_0000163978"
FT REGION 39..42
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 167..171
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 245..250
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 278..285
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 312..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 16..21
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 105
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:3D3Q"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3D3Q"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:3D3Q"
FT TURN 56..61
FT /evidence="ECO:0007829|PDB:3D3Q"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 78..94
FT /evidence="ECO:0007829|PDB:3D3Q"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:3D3Q"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:3D3Q"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 207..223
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:3D3Q"
FT TURN 247..251
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 252..257
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 262..286
FT /evidence="ECO:0007829|PDB:3D3Q"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:3D3Q"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:3D3Q"
FT HELIX 300..314
FT /evidence="ECO:0007829|PDB:3D3Q"
SQ SEQUENCE 332 AA; 38526 MW; 8AFDFCA1DE3F9F55 CRC64;
MTEMTKPFLI VIVGPTASGK TELSIEVAKK FNGEIISGDS MQVYQGMDIG TAKVTTEEME
GIPHYMIDIL PPDASFSAYE FKKRAEKYIK DITRRGKVPI IAGGTGLYIQ SLLYNYAFED
ESISEDKMKQ VKLKLKELEH LNNNKLHEYL ASFDKESAKD IHPNNRKRVL RAIEYYLKTK
KLLSSRKKVQ QFTENYDTLL IGIEMSRETL YLRINKRVDI MLGHGLFNEV QHLVEQGFEA
SQSMQAIGYK ELVPVIKGNI SMENAVEKLK QHSRQYAKRQ LTWFKNKMNV HWLNKERMSL
QMMLDEITTQ INKRSSNHDC KRKHPRPSTR EL
