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EBIDatabasesDatabase BrowsingDbfetch

EBI Dbfetch

ID   Y10549; SV 1; linear; genomic DNA; STD; PRO; 586 BP.
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AC   Y10549;
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DT   18-JUL-1997 (Rel. 52, Created)
DT   14-NOV-2006 (Rel. 89, Last updated, Version 4)
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DE   B.stearothermophilus fms gene
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KW   fms gene; N-formylmethionylaminoacyl-tRNA deformylase.
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OS   Geobacillus stearothermophilus
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
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RN   [1]
RX   DOI; 10.1006/jmbi.1997.0904
RX   PUBMED; 9126850.
RA   Meinnel T., Lazennec C., Villoing S., Blanquet S.;
RT   "Structure-function relationships within the peptide deformylase family.
RT   Evidence for a conserved architecture of the active site involving three
RT   conserved motifs and a metal ion";
RL   J. Mol. Biol. 267(3):749-761(1997).
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RN   [2]
RP   1-586
RA   Meinnel T.;
RT   ;
RL   Submitted (15-JAN-1997) to the EMBL/GenBank/DDBJ databases.
RL   T. Meinnel, Laboratoire de Biochimia, Ecole Polytechnique, 91128 Palaiseau,
RL   FRANCE
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RN   [3]
RX   DOI; 10.1111/j.1432-1033.1990.tb19432.x
RX   PUBMED; 2253629.
RA   Borges A., Hawkins C.F., Perham R.N.;
RT   "Cloning and sequence analysis of the genes encoding the dihydrolipoamide
RT   acetyltransferase and dihydrolipoamide dehydrogenase components of the
RT   pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus";
RL   Eur. J. Biochem. 194(1):95-102(1990).
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FH   Key             Location/Qualifiers
FH
FT   source          1..586
FT                   /organism="Geobacillus stearothermophilus"
FT                   /strain="ATCC 1518"
FT                   /mol_type="genomic DNA"
FT                   /db_xref="taxon:1422"
FT   CDS             28..582
FT                   /transl_table=11
FT                   /gene="fms"
FT                   /product="N-formylmethionylaminoacyl-tRNA deformylase"
FT                   /EC_number="3.5.1.27"
FT                   /db_xref="GOA:O31410"
FT                   /db_xref="InterPro:IPR000181"
FT                   /db_xref="PDB:1LQY"
FT                   /db_xref="UniProtKB/Swiss-Prot:O31410"
FT                   /protein_id="CAA71581.1"
FT                   /translation="MITMKDIIKEGHPTLRKVAEPVPLPPSEEDKRILQSLLDYVKMSQ
FT                   DPELAAKYGLRPGIGLAAPQINVSKRMIAVHVTDENGTLYSYALFNPKIVSHSVQQCYL
FT                   TTGEGCLSVDRDVPGYVLRYARITVTGTTLDGEEVTLRLKGLPAIVFQHEIDHLNGIMF
FT                   YDRINPADPFQVPDGAIPIGR"
FT   conflict        197..199
FT                   /replace="cg"
FT                   /citation=[3]
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SQ   Sequence 586 BP; 146 A; 164 C; 160 G; 115 T; 1 other;
     atgcgagaga caggagtgaa aaggcgaatg atcaccatga aagatatcat taaagaaggg        60
     catccgacgc tgcggaaagt ggctgagccc gttccgctgc cgccttcaga ggaagacaaa       120
     cgcattttgc aaagcttgct tgactatgtg aaaatgagcc aagatccgga actggcggcc       180
     aaatacggcc tgcggccngg catcggcctc gccgctccgc aaatcaacgt ctccaaacgg       240
     atgattgccg ttcatgtcac tgatgaaaac ggaacgctgt acagctatgc cttgttcaat       300
     ccgaaaatcg tcagccactc tgtgcagcaa tgttatttga cgacggggga aggctgcctg       360
     tcggtcgacc gtgatgtgcc cggatacgta ctgcgctatg cccgcatcac ggtcaccggc       420
     acgacgctcg acggcgagga agtcaccttg cgcctcaaag gattgccggc catcgtcttc       480
     cagcatgaaa tcgaccattt aaacggcatt atgttttatg accgcatcaa tccggccgac       540
     ccgttccaag tgccagacgg ggcgatcccg atcgggcgct gaaccg                      586
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