MIAA2_PELPD
ID MIAA2_PELPD Reviewed; 313 AA.
AC A1AU18;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=tRNA dimethylallyltransferase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=DMAPP:tRNA dimethylallyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=DMATase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=IPP transferase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=IPPT 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=IPTase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
GN Name=miaA2 {ECO:0000255|HAMAP-Rule:MF_00185}; OrderedLocusNames=Ppro_3245;
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000482; ABL00839.1; -; Genomic_DNA.
DR RefSeq; WP_011737056.1; NC_008609.1.
DR AlphaFoldDB; A1AU18; -.
DR SMR; A1AU18; -.
DR STRING; 338966.Ppro_3245; -.
DR PRIDE; A1AU18; -.
DR EnsemblBacteria; ABL00839; ABL00839; Ppro_3245.
DR KEGG; ppd:Ppro_3245; -.
DR eggNOG; COG0324; Bacteria.
DR HOGENOM; CLU_032616_0_1_7; -.
DR OMA; LEIAIHQ; -.
DR OrthoDB; 1069591at2; -.
DR Proteomes; UP000006732; 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..313
FT /note="tRNA dimethylallyltransferase 2"
FT /id="PRO_0000377258"
FT REGION 41..44
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT REGION 161..165
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 16..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 18..23
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 106
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ SEQUENCE 313 AA; 35962 MW; C80A5C417F9FC509 CRC64;
MNVSNAPRFN LLTILGPTAS GKTRLAVNLA RELGGEIISA DSRQVFRRMD IGTGKDLHEY
GEVHHHLIDI LEPGEEFSVF AFQRLFLEAV GDICGRGRLP LLCGGTGMYL DAALRRYRMH
EVPEDREWRA SLEGVGDGEL ASRLREFRPG LHNSTDLVDR QRTIRALEIA RFQADCAGDD
EPFPDLRPLV IGIRWERAEL RRRITERLRQ RLESGMIEEV RRLNDGGVPW ERLDYYGLEY
RFVGMYLRDE LSRNDLFQKL NSAIHDFAKR QETWFRRMER NGVAINWVDG GGGPLSEARR
VILDNSYHLA TGR