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P96275 (DEF_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptide deformylase
Short name=PDF
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase
Gene names
Name:def
Ordered Locus Names:Rv0429c, MT0444
ORF Names:MTCY22G10.26c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions By similarity. HAMAP-Rule MF_00163

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP-Rule MF_00163

Cofactor

Binds 1 Fe2+ ion By similarity.

Miscellaneous

Was identified as a high-confidence drug target. HAMAP-Rule MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082806

Sites

Active site1491 By similarity
Metal binding1061Iron By similarity
Metal binding1481Iron By similarity
Metal binding1521Iron By similarity

Secondary structure

1 ........................... 197
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P96275 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 14F2F655EDF01C93

FASTA19720,939
        10         20         30         40         50         60 
MAVVPIRIVG DPVLHTATTP VTVAADGSLP ADLAQLIATM YDTMDAANGV GLAANQIGCS 

        70         80         90        100        110        120 
LRLFVYDCAA DRAMTARRRG VVINPVLETS EIPETMPDPD TDDEGCLSVP GESFPTGRAK 

       130        140        150        160        170        180 
WARVTGLDAD GSPVSIEGTG LFARMLQHET GHLDGFLYLD RLIGRYARNA KRAVKSHGWG 

       190 
VPGLSWLPGE DPDPFGH

« Hide

References

[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842573 Genomic DNA. Translation: CAB06569.1.
AE000516 Genomic DNA. Translation: AAK44667.1.
AL123456 Genomic DNA. Translation: CCP43160.1.
PIRC70631.
RefSeqNP_214943.1. NC_000962.3.
NP_334853.1. NC_002755.2.
YP_006513755.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3E3UX-ray1.56A1-197[»]
ProteinModelPortalP96275.
SMRP96275. Positions 2-197.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv0429c.

Proteomic databases

PRIDEP96275.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK44667; AAK44667; MT0444.
GeneID13318296.
886366.
923753.
KEGGmtc:MT0444.
mtu:Rv0429c.
mtv:RVBD_0429c.
PATRIC18122688. VBIMycTub22151_0478.

Organism-specific databases

TubercuListRv0429c.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243508.
KOK01462.
OMALIGRWKR.
ProtClustDBPRK00150.

Family and domain databases

Gene3D3.90.45.10. 1 hit.
HAMAPMF_00163. Pep_deformylase.
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERPTHR10458. PTHR10458. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. Fmet_deformylase. 1 hit.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Other

BindingDBP96275.
ChEMBLCHEMBL5765.
EvolutionaryTraceP96275.

Entry information

Entry nameDEF_MYCTU
AccessionPrimary (citable) accession number: P96275
Secondary accession number(s): L0T3J0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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