Reviewed, UniProtKB/Swiss-Prot Q8AAP4 (DEF_BACTN)

Names and origin

Protein names

Recommended name:
    Peptide deformylase
      Short name=PDF
    EC=3.5.1.88
Alternative name(s):
    Polypeptide deformylase

Gene names

Name:	def
Ordered Locus Names:	BT_0420

Organism

Bacteroides thetaiotaomicron [Complete proteome] [HAMAP]

Taxonomic identifier

818 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

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
Cofactor	Binds 1 Fe2+ ion By similarity. HAMAP MF_00163
Sequence similarities	Belongs to the polypeptide deformylase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Ligand	Iron Metal-binding
Molecular function	Hydrolase
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: UniProtKB-KW 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
Molecule processing
	Chain	1 – 184	184	Peptide deformylase HAMAP MF_00163		PRO_0000082741
Sites
	Active site	141	1	By similarity
	Metal binding	98	1	Iron By similarity
	Metal binding	140	1	Iron By similarity
	Metal binding	144	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8AAP4-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 0C161E8636B0DCC6	FASTA	184	21,013
	10 20 30 40 50 60 MILPIYVYGQ PVLRKVAEDI TPEYPNLKEL IANMFETMVH ADGVGLAAPQ IGLPIRVVTI 70 80 90 100 110 120 TLDPLSEDYP EFKDFNKAYI NPHIIEVGGE EVSMEEGCLS LPGIHESVKR GNKIRVKYMD 130 140 150 160 170 180 ENFVEHDEVV EGYLARVMQH EFDHLDGKMF IDHLSPLRKQ MIRGKLNTML KGKARSSYKM KQVK

References

[1]

"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis." Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I. Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015928 Genomic DNA. Translation: AAO75527.1.
RefSeq	NP_809333.1.
3D structure databases
SMR	Q8AAP4. Positions 1-156.
ModBase	Search...
Genome annotation databases
GeneID	1074758.
GenomeReviews	Gene locus BT_0420 in contig AE015928_GR.
KEGG	bth:BT_0420.
NMPDR	fig|226186.1.peg.420.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG665227.
OMA	KELIANM.
PhylomeDB	Q8AAP4.
Enzyme and pathway databases
BioCyc	BTHE226186:BT_0420-MONOMER.
BRENDA	3.5.1.88. 21018.
Family and domain databases
HAMAP	MF_00163. Pep_deformylase. [Tree]
InterPro	IPR000181. Fmet_deformylase. [Graphical view]
Gene3D	G3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
PANTHER	PTHR10458. Fmet_deformylase. 1 hit.
Pfam	PF01327. Pep_deformylase. 1 hit. [Graphical view]
PIRSF	PIRSF004749. Pep_def. 1 hit.
PRINTS	PR01576. PDEFORMYLASE.
TIGRFAMs	TIGR00079. pept_deformyl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DEF_BACTN

Accession

Primary (citable) accession number: Q8AAP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)