(data stored in ACNUC7421 zone)

SWISSPROT: MIAA_PSEHT

ID   MIAA_PSEHT              Reviewed;         306 AA.
AC   Q3IDT9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 77.
DE   RecName: Full=tRNA dimethylallyltransferase {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 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=DMAPP:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=DMATase {ECO:0000255|HAMAP-Rule:MF_00185};
DE   AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPP transferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPPT {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPTase {ECO:0000255|HAMAP-Rule:MF_00185};
GN   Name=miaA {ECO:0000255|HAMAP-Rule:MF_00185};
GN   OrderedLocusNames=PSHAa0270;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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: Dimethylallyl diphosphate + adenine(37) in
CC       tRNA = diphosphate + N(6)-dimethylallyladenine(37) in tRNA.
CC       {ECO:0000255|HAMAP-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.
CC       {ECO:0000255|HAMAP-Rule:MF_00185}.
DR   EMBL; CR954246; CAI85369.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q3IDT9; -.
DR   SMR; Q3IDT9; -.
DR   STRING; 326442.PSHAa0270; -.
DR   EnsemblBacteria; CAI85369; CAI85369; PSHAa0270.
DR   KEGG; pha:PSHAa0270; -.
DR   eggNOG; ENOG4105DKX; Bacteria.
DR   eggNOG; COG0324; LUCA.
DR   HOGENOM; HOG000039996; -.
DR   KO; K00791; -.
DR   OMA; GTGLYIR; -.
DR   OrthoDB; POG091H00NK; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   HAMAP; MF_00185; IPP_trans; 1.
DR   InterPro; IPR018022; IPP_trans.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11088:SF43; PTHR11088:SF43; 1.
DR   Pfam; PF01715; IPPT; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00174; miaA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IDT9.
DR   SWISS-2DPAGE; Q3IDT9.
KW   ATP-binding; Complete proteome; Magnesium; Nucleotide-binding;
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN         1    306       tRNA dimethylallyltransferase.
FT                                /FTId=PRO_1000020644.
FT   NP_BIND      12     19       ATP. {ECO:0000255|HAMAP-Rule:MF_00185}.
FT   REGION       14     19       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00185}.
FT   REGION       37     40       Interaction with substrate tRNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00185}.
FT   REGION      161    165       Interaction with substrate tRNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00185}.
FT   REGION      242    247       Interaction with substrate tRNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00185}.
FT   SITE        103    103       Interaction with substrate tRNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00185}.
FT   SITE        125    125       Interaction with substrate tRNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00185}.
SQ   SEQUENCE   306 AA;  34770 MW;  98D6ADC9D4632BE5 CRC64;
     MLSNLPVIFL MGPTAAGKTA LAISLCEHLN TEIISVDSAL VYKGMDIGTA KPDASELARA
     PHHLIDLLDP SETYSVADFR RDAIIKIDEF HQQGKVPVLV GGTMLYFKAL IDGLSPLPEA
     NVEIRAELEA QAAQYGWPHL YQELVKIDPQ AAQKMSENDS QRINRALEVY KLTGKTMTEL
     QKQKQPVLPY TFHQFAIAPT QRSELHQRIE KRFKIMLEQG FENEVSTLYL RKDLHPNMPS
     IRCVGYRQMW DYLAGEIDHD EMVFRGIAAT RQLAKRQLTW LRSWPDVTWL TTGDEENLHR
     VVSSLS
//

If you have problems or comments...

PBIL Back to PBIL home page