MIAA1_PORGI
ID MIAA1_PORGI Reviewed; 300 AA.
AC Q7MAW8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=tRNA dimethylallyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE EC=2.5.1.75 {ECO:0000255|HAMAP-Rule:MF_00185};
DE AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=DMAPP:tRNA dimethylallyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=DMATase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=IPP transferase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=IPPT 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=IPTase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
GN Name=miaA1 {ECO:0000255|HAMAP-Rule:MF_00185}; OrderedLocusNames=PG_0335;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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:0000255|HAMAP-Rule:MF_00185}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00185};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00185}.
CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000255|HAMAP-
CC Rule:MF_00185}.
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DR EMBL; AE015924; AAQ65548.1; -; Genomic_DNA.
DR RefSeq; WP_005874242.1; NC_002950.2.
DR AlphaFoldDB; Q7MAW8; -.
DR SMR; Q7MAW8; -.
DR STRING; 242619.PG_0335; -.
DR EnsemblBacteria; AAQ65548; AAQ65548; PG_0335.
DR KEGG; pgi:PG_0335; -.
DR PATRIC; fig|242619.8.peg.309; -.
DR eggNOG; COG0324; Bacteria.
DR HOGENOM; CLU_032616_0_1_10; -.
DR OMA; YAKRQYT; -.
DR OrthoDB; 1069591at2; -.
DR BioCyc; PGIN242619:G1G02-315-MON; -.
DR Proteomes; UP000000588; 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 3: Inferred from homology;
KW ATP-binding; Magnesium; Nucleotide-binding; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..300
FT /note="tRNA dimethylallyltransferase 1"
FT /id="PRO_0000163951"
FT REGION 38..41
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 13..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 15..20
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 104
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 126
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ SEQUENCE 300 AA; 34694 MW; 0980D939FF878627 CRC64;
METQDHTLYV LLGPTGVGKT DLSLDIAERL GSPIISADSR QIFRELPIGT AAPTPEQRAK
VPHLFVGTHS VRDYYSAGMY EVEVLEALKE LFRKYRGVLL TGGSMMYIDA VCRGIDDIPD
PFPEVREELY ARYAAEGLDG ILAQLRLLDP DYYAKVDRRN YKRVIHGLEI CLSTGRPFSS
FHRHEAKERP FRIVKIGLYR EREELCKRID ARVLEMMEQG LEEEARAVYP LRHLNALNTV
GYKEMFEYFD GSIDRAEAVR RIQRNSRVYA RKQMTWFRRD STIRWFHPEA DKGTVLTLVT
