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B7HLK0 (B7HLK0_BACC7) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptide deformylase 1 HAMAP MF_00163
Short name=PDF 1 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase 1 HAMAP MF_00163
Gene names
Name:def1 HAMAP MF_00163 EMBL ACJ78821.1
Ordered Locus Names:BCAH187_A3915
OrganismBacillus cereus (strain AH187) [Complete proteome] [HAMAP]
Taxonomic identifier405534 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 MF_00163

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP MF_00163 SAAS SAAS000181

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family. HAMAP MF_00163 RuleBase RU003335

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1331 By similarity HAMAP MF_00163
Metal binding901Iron By similarity HAMAP MF_00163
Metal binding1321Iron By similarity HAMAP MF_00163
Metal binding1361Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
B7HLK0 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: ED6ED75C2A963C8D

FASTA15617,422
        10         20         30         40         50         60 
MAVLEIVKHP NEVLETPCER VINFDKKLVK LLKDMHETML IADGVGLAAP QVGVSLQVAV 

        70         80         90        100        110        120 
VDIGDDTGKI ELINPSILEK RGEQVGPEGC LSFPGLYGEV ERADYIKVRA QNRRGKVFLL 

       130        140        150 
EAEGFLARAI QHEIDHLHGV LFTSKVTRYY EENELE

« Hide

References

[1]"Genome sequence of Bacillus cereus AH187."
Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., Okstad O.A., Ravel J., Sutton G.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001177 Genomic DNA. Translation: ACJ78821.1.
RefSeqYP_002339855.1. NC_011658.1.

3D structure databases

ProteinModelPortalB7HLK0.
SMRB7HLK0. Positions 1-151.
ModBaseSearch...

Protein-protein interaction databases

STRINGB7HLK0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000091929; EBBACP00000090211; EBBACG00000091922.
GeneID7077344.
GenomeReviewsGene locus BCAH187_A3915 in contig CP001177_GR.
KEGGbcr:BCAH187_A3915.
PATRIC18833265. VBIBacCer120511_4103.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000001175.
HOGENOMHBG665227.
OMARQLAKEM.
ProtClustDBPRK12846.

Family and domain databases

HAMAPMF_00163. Pep_deformylase.
[Tree]
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
KOK01462.
PANTHERPTHR10458. Fmet_deformylase. 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...

Entry information

Entry nameB7HLK0_BACC7
AccessionPrimary (citable) accession number: B7HLK0
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: December 14, 2011
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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