Peptide deformylase 2 - Bacillus cereus (strain ZK / E33L)

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Q635V4 (Q635V4_BACCZ) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 48. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Peptide deformylase 2 HAMAP MF_00163
Short name=PDF 2 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163

Alternative name(s):
Polypeptide deformylase 2 HAMAP MF_00163

Gene names

Name:	def EMBL AAU16534.1
Synonyms:	def2 HAMAP MF_00163
Ordered Locus Names:	BCE33L3732

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP] EMBL AAU16534.1

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Protein existence	Inferred 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

Ontologies

Keywords
Biological process	Protein biosynthesis SAAS SAAS000181 HAMAP MF_00163
Ligand	Iron HAMAP MF_00163 Metal-binding HAMAP MF_00163 SAAS SAAS000181
Molecular function	Hydrolase HAMAP MF_00163 SAAS SAAS000181 EMBL AAU16534.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: HAMAP
Molecular function	iron ion binding Inferred from electronic annotation. Source: InterPro peptide deformylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Active site

154

By similarity HAMAP MF_00163

Metal binding

110

Iron By similarity HAMAP MF_00163

Metal binding

153

Iron By similarity HAMAP MF_00163

Metal binding

157

Iron By similarity HAMAP MF_00163

Sequences

Sequence

Length

Mass (Da)

Tools

Q635V4 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: EC08DDB6E5D6D78D
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FASTA

184

20,529

        10         20         30         40         50         60 
MLTMKDVIRE GDPILRKVAE EVVIPASKED TNTLKEMIEF VINSQDPEMA EKYSLRPGIG 

        70         80         90        100        110        120 
LAAPQIGISK KMIAVHVTDT DGTLYSHALF NPKIISHSVE RTYLQSGEGC LSVDREVPGY 

       130        140        150        160        170        180 
VPRYTRITVK ATSINGEEVK LRLKGLPAIV FQHEIDHLNG VMFYDHINKE NPFAAPDGSK 


PLER

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References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis."
Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P.

Gilna P.
J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000001 Genomic DNA. Translation: AAU16534.1.
RefSeq	YP_085313.1. NC_006274.1.
3D structure databases
ProteinModelPortal	Q635V4.
SMR	Q635V4. Positions 1-184.
ModBase	Search...
Protein-protein interaction databases
STRING	Q635V4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000041660; EBBACP00000040561; EBBACG00000041651.
GeneID	3024137.
GenomeReviews	Gene locus BCE33L3732 in contig CP000001_GR.
KEGG	bcz:BCZK3732.
PATRIC	18891222. VBIBacCer95304_3949.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0242.
GeneTree	EBGT00050000001175.
HOGENOM	HBG665227.
OMA	ADGEGCL.
ProtClustDB	PRK00150.
Family and domain databases
HAMAP	MF_00163. Pep_deformylase. [Tree]
InterPro	IPR000181. Fmet_deformylase. IPR023635. Peptide_deformylase. [Graphical view]
Gene3D	G3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
KO	K01462.
PANTHER	PTHR10458. Fmet_deformylase. 1 hit.
Pfam	PF01327. Pep_deformylase. 1 hit. [Graphical view]
PIRSF	PIRSF004749. Pep_def. 1 hit.
PRINTS	PR01576. PDEFORMYLASE.
SUPFAM	SSF56420. Fmet_deformylase. 1 hit.
TIGRFAMs	TIGR00079. Pept_deformyl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

Q635V4_BACCZ

Accession

Primary (citable) accession number: Q635V4

Entry history

Integrated into UniProtKB/TrEMBL:	October 25, 2004
Last sequence update:	October 25, 2004
Last modified:	December 14, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information