(data stored in SCRATCH3701 zone)

SWISSPROT: MIAA_SYNS3

ID   MIAA_SYNS3              Reviewed;         310 AA.
AC   Q0IDZ4;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 90.
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}; OrderedLocusNames=sync_0091;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(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). {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}.
DR   EMBL; CP000435; ABI47681.1; -; Genomic_DNA.
DR   RefSeq; WP_011618078.1; NC_008319.1.
DR   SMR; Q0IDZ4; -.
DR   STRING; 64471.sync_0091; -.
DR   EnsemblBacteria; ABI47681; ABI47681; sync_0091.
DR   KEGG; syg:sync_0091; -.
DR   eggNOG; ENOG4105DKX; Bacteria.
DR   eggNOG; COG0324; LUCA.
DR   HOGENOM; HOG000039996; -.
DR   KO; K00791; -.
DR   OMA; YAKRQFT; -.
DR   OrthoDB; 1069591at2; -.
DR   BioCyc; SSP64471:G1G72-94-MONOMER; -.
DR   Proteomes; UP000001961; 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   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   Pfam; PF01715; IPPT; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00174; miaA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0IDZ4.
DR   SWISS-2DPAGE; Q0IDZ4.
KW   ATP-binding; Magnesium; Nucleotide-binding; Reference proteome;
KW   Transferase; tRNA processing.
FT   CHAIN           1..310
FT                   /note="tRNA dimethylallyltransferase"
FT                   /id="PRO_0000377344"
FT   NP_BIND         24..31
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   REGION          26..31
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   REGION          49..52
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            115
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   310 AA;  34056 MW;  6EC890525F78B001 CRC64;
     MNQINSEFGP DAGAKAPLVV ALVGPTASGK TALALELAEH FQLEILNIDS RQLYREMDIG
     TAKPTAEQQQ RVTHHLLDLR SPDQPITLQE FQQEATAAVS QVLKERGVAF LAGGSGLYLK
     ALTQGLQPPA VPPQAELRRQ LSSLGQANCH QLLQQADPQA AAKIAPADAV RTQRALEVLY
     SSGKPMSAQQ STNPPPWRVL ELGLNPMELR SRIAQRTLQI YQEGLLEETR QLSQRYGPDL
     PMLQTIGYGE ALEVLQGGLS EAQAIATTTR RTQQFAKRQR TWFRRQHSPH WLTGQDALSE
     AIRLIEAGLG
//

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