ID   MIAA_ALCBS              Reviewed;         329 AA.
AC   Q0VME6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=tRNA Delta(2)-isopentenylpyrophosphate transferase;
DE            Short=IPP transferase;
DE            EC=2.5.1.8;
DE   AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase;
DE            Short=IPTase;
DE            Short=IPPT;
DE   AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase;
DE            Short=DMAPP:tRNA dimethylallyltransferase;
DE            Short=DMATase;
GN   Name=miaA; OrderedLocusNames=ABO_2204;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + tRNA = diphosphate +
CC       tRNA containing 6-isopentenyladenosine.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the IPP transferase family.
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DR   EMBL; AM286690; CAL17652.1; -; Genomic_DNA.
DR   RefSeq; YP_693924.1; -.
DR   GeneID; 4211582; -.
DR   GenomeReviews; AM286690_GR; ABO_2204.
DR   KEGG; abo:ABO_2204; -.
DR   NMPDR; fig|393595.12.peg.2203; -.
DR   HOGENOM; Q0VME6; -.
DR   OMA; Q0VME6; VNADSMQ.
DR   BioCyc; ABOR393595:ABO_2204-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004811; F:tRNA isopentenyltransferase activity; IEA:HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:HAMAP.
DR   HAMAP; MF_00185; -; 1.
DR   InterPro; IPR002627; IPPT.
DR   InterPro; IPR018022; tRNA_delta_PyrP_Trfase.
DR   PANTHER; PTHR11088; IPPT; 1.
DR   Pfam; PF01715; IPPT; 1.
DR   ProDom; PD004674; IPPT; 1.
DR   ProDom; PD005388; IPPtrans_like; 1.
DR   TIGRFAMs; TIGR00174; miaA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Magnesium; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase; tRNA processing.
FT   CHAIN         1    329       tRNA Delta(2)-isopentenylpyrophosphate
FT                                transferase.
FT                                /FTId=PRO_1000020559.
FT   NP_BIND      14     21       ATP (Potential).
FT   REGION       16     21       Substrate binding (By similarity).
FT   REGION       39     42       Interaction with substrate tRNA (By
FT                                similarity).
FT   REGION      163    167       Interaction with substrate tRNA (By
FT                                similarity).
FT   SITE        105    105       Interaction with substrate tRNA (By
FT                                similarity).
FT   SITE        127    127       Interaction with substrate tRNA (By
FT                                similarity).
SQ   SEQUENCE   329 AA;  36537 MW;  8078F24D5BF339C2 CRC64;
     MMPEASLPIL LLMGPTCSGK TALAIEAAQT LPIEIINVDS ALVYKGLNIG AARPTEEELA
     LAPHRLLGFR DLTEPYSAAD FRADALKHIE QIHNNGKLPL LVGGTVLYFK ALVEGLAPLP
     EADPVVRAEI AALADAQGWP AVHQALAEVD PVTAARLKPT DKQRLQRALE VFRLTGRPLA
     AFHAEHDKTL TKSRDGLSQF SGLPYPVLST ALAPQDRAWL HEQIALRFRA MLNSGLQEEV
     EALRQQPQLN ADLPGIRAVG YRQMWEYLDG MYGYDSMVER GIIATRQLAK RQFTWLRKWP
     ELQWFDSNDR SQRDALFGLL AKNCKSVFS
//