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MIAA_PSEAE
ID   MIAA_PSEAE              Reviewed;         323 AA.
AC   Q9HUL9;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=tRNA dimethylallyltransferase;
DE            EC=2.5.1.75;
DE   AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase;
DE            Short=DMAPP:tRNA dimethylallyltransferase;
DE            Short=DMATase;
DE   AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase;
DE            Short=IPP transferase;
DE            Short=IPPT;
DE            Short=IPTase;
GN   Name=miaA; OrderedLocusNames=PA4945;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PYROPHOSPHATE.
RX   PubMed=17292915; DOI=10.1016/j.jmb.2007.01.048;
RA   Xie W., Zhou C., Huang R.H.;
RT   "Structure of tRNA dimethylallyltransferase: RNA modification through a
RT   channel.";
RL   J. Mol. Biol. 367:872-881(2007).
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).
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG08330.1; -; Genomic_DNA.
DR   PIR; E83028; E83028.
DR   RefSeq; NP_253632.1; NC_002516.2.
DR   RefSeq; WP_003113929.1; NZ_QZGE01000002.1.
DR   PDB; 3CRM; X-ray; 1.90 A; A=1-323.
DR   PDB; 3CRQ; X-ray; 2.20 A; A=1-323.
DR   PDB; 3CRR; X-ray; 1.90 A; A=1-323.
DR   PDBsum; 3CRM; -.
DR   PDBsum; 3CRQ; -.
DR   PDBsum; 3CRR; -.
DR   AlphaFoldDB; Q9HUL9; -.
DR   SMR; Q9HUL9; -.
DR   STRING; 287.DR97_2298; -.
DR   PaxDb; Q9HUL9; -.
DR   PRIDE; Q9HUL9; -.
DR   DNASU; 878016; -.
DR   EnsemblBacteria; AAG08330; AAG08330; PA4945.
DR   GeneID; 878016; -.
DR   KEGG; pae:PA4945; -.
DR   PATRIC; fig|208964.12.peg.5178; -.
DR   PseudoCAP; PA4945; -.
DR   HOGENOM; CLU_032616_0_0_6; -.
DR   InParanoid; Q9HUL9; -.
DR   OMA; YAKRQYT; -.
DR   PhylomeDB; Q9HUL9; -.
DR   BioCyc; PAER208964:G1FZ6-5061-MON; -.
DR   EvolutionaryTrace; Q9HUL9; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
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; 1.
DR   TIGRFAMs; TIGR00174; miaA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Magnesium; Nucleotide-binding;
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..323
FT                   /note="tRNA dimethylallyltransferase"
FT                   /id="PRO_0000163956"
FT   REGION          37..40
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000250"
FT   REGION          161..165
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000250"
FT   REGION          253..258
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000250"
FT   REGION          286..293
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000250"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         14..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            103
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000250"
FT   SITE            125
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000250"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   HELIX           18..28
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   TURN            38..41
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   HELIX           54..59
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   STRAND          62..66
FT                   /evidence="ECO:0007829|PDB:3CRQ"
FT   HELIX           76..92
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   STRAND          96..102
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   HELIX           104..111
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   STRAND          201..209
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   HELIX           213..229
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   HELIX           232..240
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   HELIX           251..253
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   HELIX           257..264
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   HELIX           270..293
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   STRAND          299..302
FT                   /evidence="ECO:0007829|PDB:3CRM"
FT   HELIX           308..318
FT                   /evidence="ECO:0007829|PDB:3CRM"
SQ   SEQUENCE   323 AA;  35769 MW;  B33DFB9EA45157CF CRC64;
     MSSLPPAIFL MGPTAAGKTD LAMALADALP CELISVDSAL IYRGMDIGTA KPSRELLARY
     PHRLIDIRDP AESYSAAEFR ADALAAMAKA TARGRIPLLV GGTMLYYKAL LEGLADMPGA
     DPEVRAAIEA EAQAEGWEAL HRQLAEVDPE SAARIHPNDP QRLMRALEVY RLGGVSMSDL
     RRRQSAEKAD FDASGRNQLP YTVAQLAIAP EQRQVLHARI AQRFRQMLEQ GFIAEVEALH
     ARSDLHAGLP SIRAVGYRQV WDYLDGKLSY AEMTERGIIA TRQLAKRQFT WLRSWSHLHW
     MDSLAGDNLP RALKYLKTVS ILA
 
 
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