ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P0A6K3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DEF_ECOLI
Primary accession number P0A6K3
Secondary accession numbers P27251 Q2M6V1
Integrated into Swiss-Prot on March 29, 2005
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 42)
Name and origin of the protein
Protein name Peptide deformylase
Synonyms PDF
EC 3.5.1.88
Polypeptide deformylase
Gene name
Name: def
Synonyms: fms
OrderedLocusNames: b3287, JW3248
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
STRAIN=K12;
PubMed=8112305 [NCBI, ExPASy, EBI, Israel, Japan]
Mazel D., Pochet S., Marliere P.;
"Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation.";
EMBO J. 13:914-923(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / K37;
PubMed=1624424 [NCBI, ExPASy, EBI, Israel, Japan]
Guillon J.-M., Mechulam Y., Schmitter J.-M., Blanquet S., Fayat G.;
"Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli.";
J. Bacteriol. 174:4294-4301(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
STRAIN=K12 / K37;
PubMed=8432722 [NCBI, ExPASy, EBI, Israel, Japan]
Meinnel T., Guillon J.-M., Mechulam Y., Blanquet S.;
"The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet) formyltransferase, escapes metabolic control.";
J. Bacteriol. 175:993-1000(1993).
[6]
CHARACTERIZATION.
PubMed=7896716 [NCBI, ExPASy, EBI, Israel, Japan]
Meinnel T., Blanquet S.;
"Enzymatic properties of Escherichia coli peptide deformylase.";
J. Bacteriol. 177:1883-1887(1995).
[7]
COFACTOR.
DOI=10.1006/bbrc.1998.8616; PubMed=9610360 [NCBI, ExPASy, EBI, Israel, Japan]
Groche D., Becker A., Schlichting I., Kabsch W., Schultz S., Wagner A.F.;
"Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site.";
Biochem. Biophys. Res. Commun. 246:342-346(1998).
[8]
STRUCTURE BY NMR.
DOI=10.1006/jmbi.1996.0521; PubMed=8845003 [NCBI, ExPASy, EBI, Israel, Japan]
Meinnel T., Blanquet S., Dardel F.;
"A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase.";
J. Mol. Biol. 262:375-386(1996).
[9]
STRUCTURE BY NMR.
DOI=10.1006/jmbi.1998.1882; PubMed=9665852 [NCBI, ExPASy, EBI, Israel, Japan]
Dardel F., Ragusa S., Lazennec C., Blanquet S., Meinnel T.;
"Solution structure of nickel-peptide deformylase.";
J. Mol. Biol. 280:501-513(1998).
[10]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
DOI=10.1021/bi9711543; PubMed=9374869 [NCBI, ExPASy, EBI, Israel, Japan]
Chan M.K., Gong W., Rajagopalan P.T.R., Hao B., Tsai C.M., Pei D.;
"Crystal structure of the Escherichia coli peptide deformylase.";
Biochemistry 36:13904-13909(1997).
[11]
ERRATUM.
Chan M.K., Gong W., Rajagopalan P.T.R., Hao B., Tsai C.M., Pei D.;
Biochemistry 37:13042-13042(1998).
[12]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1074/jbc.273.19.11413; PubMed=9565550 [NCBI, ExPASy, EBI, Israel, Japan]
Becker A., Schlichting I., Kabsch W., Schultz S., Wagner A.F.;
"Structure of peptide deformylase and identification of the substrate binding site.";
J. Biol. Chem. 273:11413-11416(1998).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1038/4162; PubMed=9846875 [NCBI, ExPASy, EBI, Israel, Japan]
Becker A., Schlichting I., Kabsch W., Groche D., Schultz S., Wagner A.F.;
"Iron center, substrate recognition and mechanism of peptide deformylase.";
Nat. Struct. Biol. 5:1053-1058(1998).
[14]
X-RAY CRYSTALLOGRAPHY.
DOI=10.1021/bi982594c; PubMed=10200158 [NCBI, ExPASy, EBI, Israel, Japan]
Hao B., Gong W., Rajagopalan P.T.R., Zhou Y., Pei D., Chan M.K.;
"Structural basis for the design of antibiotics targeting peptide deformylase.";
Biochemistry 38:4712-4719(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X77800; CAA54826.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X63666; CAA45206.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X65946; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X77091; CAA54367.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U18997; AAA58084.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76312.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78005.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S23107; S23107.
RefSeq AP_004504.1; -.
NP_417745.1; -.
3D structure databases
PDB
1BS4; X-ray; 1.90 A; A/B/C=1-169.[ExPASy / RCSB / EBI]
1BS5; X-ray; 2.50 A; A/B/C=1-169.[ExPASy / RCSB / EBI]
1BS6; X-ray; 2.10 A; A/B/C=1-169.[ExPASy / RCSB / EBI]
1BS7; X-ray; 2.50 A; A/B/C=1-169.[ExPASy / RCSB / EBI]
1BS8; X-ray; 2.20 A; A/B/C=1-169.[ExPASy / RCSB / EBI]
1BSJ; X-ray; 3.00 A; A=1-169.[ExPASy / RCSB / EBI]
1BSK; X-ray; 3.00 A; A=1-169.[ExPASy / RCSB / EBI]
1BSZ; X-ray; 1.90 A; A/B/C=1-169.[ExPASy / RCSB / EBI]
1DEF; NMR; -; A=1-148.[ExPASy / RCSB / EBI]
1DFF; X-ray; 2.88 A; A=1-165.[ExPASy / RCSB / EBI]
1DTF; Model; -; A=1-169.[ExPASy / RCSB / EBI]
1G27; X-ray; 2.10 A; A/B/C=1-169.[ExPASy / RCSB / EBI]
1G2A; X-ray; 1.75 A; A/B/C=1-169.[ExPASy / RCSB / EBI]
1ICJ; X-ray; 1.90 A; A/B/C=1-169.[ExPASy / RCSB / EBI]
1LRU; X-ray; 2.10 A; A/B/C=1-169.[ExPASy / RCSB / EBI]
1XEM; X-ray; 1.76 A; A=1-169.[ExPASy / RCSB / EBI]
1XEN; X-ray; 1.85 A; A=1-169.[ExPASy / RCSB / EBI]
1XEO; X-ray; 1.30 A; A=1-169.[ExPASy / RCSB / EBI]
2AI8; X-ray; 1.70 A; A/B/C=2-169.[ExPASy / RCSB / EBI]
2DEF; NMR; -; A=3-148.[ExPASy / RCSB / EBI]
2DTF; Model; -; A=1-169.[ExPASy / RCSB / EBI]
2VHM; X-ray; 3.74 A; 5=148-162.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BS4; -.
1BS5; -.
1BS6; -.
1BS7; -.
1BS8; -.
1BSJ; -.
1BSK; -.
1BSZ; -.
1DEF; -.
1DFF; -.
1DTF; -.
1G27; -.
1G2A; -.
1ICJ; -.
1LRU; -.
1XEM; -.
1XEN; -.
1XEO; -.
2AI8; -.
2DEF; -.
2DTF; -.
2VHM; -.
ModBase P0A6K3.
Protein-protein interaction databases
IntAct P0A6K3; 9.
Enzyme and pathway databases
BioCyc EcoCyc:EG11440-MON; -.
MetaCyc:EG11440-MON; -.
Organism-specific databases
EchoBASE EB1410; -.
EcoGene EG11440; def.
Ontologies
GO
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0042586; Molecular function: peptide deformylase activity (inferred from electronic annotation from HAMAP).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006412; Biological process: translation (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00163; -; 1.
PBIL [Tree]
InterPro IPR000181; Fmet_deformylase.
Graphical view of domain structure.
Gene3D G3DSA:3.90.45.10; Fmet_deformylase; 1.
PANTHER PTHR10458; Fmet_deformylase; 1.
Pfam PF01327; Pep_deformylase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF004749; Pep_def; 1.
PRINTS PR01576; PDEFORMYLASE.
ProDom PD003844; Fmet_deformylase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00079; pept_deformyl; 1.
Genome annotation databases
GeneID 947780; -.
GenomeReviews AP009048_GR; JW3248.
U00096_GR; b3287.
KEGG ecj:JW3248; -.
eco:b3287; -.
Phylogenomic databases
HOGENOM P0A6K3; -.
Other
BindingDB P0A6K3; -.
LinkHub P0A6K3; -.
Genome annotation databases
CMR P0A6K3; b3287.
Other
ProtoNet P0A6K3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Hydrolase; Iron; Metal-binding; Protein biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   169  168     Peptide deformylase. PRO_0000082779
ACT_SITE   134   134         
METAL   91    91        Iron. 
METAL   133   133        Iron. 
METAL   137   137        Iron. 
HELIX   12    15  4      
HELIX   26    41  16      
STRAND   45    48  4      
HELIX   49    52  4      
STRAND   56    61  6      
STRAND   71    82  12      
STRAND   105   112  8      
STRAND   118   124  7      
HELIX   125   137  13      
TURN   138   140  3      
HELIX   143   146  4      
HELIX   149   166  18      
Sequence information
Length: 169 AA [This is the length of the unprocessed precursor] Molecular weight: 19328 Da [This is the MW of the unprocessed precursor] CRC64: C485EB6C1D2D91B8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSVLQVLHIP DERLRKVAKP VEEVNAEIQR IVDDMFETMY AEEGIGLAAT QVDIHQRIIV 

        70         80         90        100        110        120 
IDVSENRDER LVLINPELLE KSGETGIEEG CLSIPEQRAL VPRAEKVKIR ALDRDGKPFE 

       130        140        150        160 
LEADGLLAIC IQHEMDHLVG KLFMDYLSPL KQQRIRQKVE KLDRLKARA 

P0A6K3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!