NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).

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).
CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H₂O = formate + methionyl peptide.
COFACTOR: Binds 1 Fe(2+) ion (By similarity).
SIMILARITY: Belongs to the polypeptide deformylase family.

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

AE000657; AAC06802.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C70352; C70352.

RefSeq

NP_213407.1; -.

3D structure databases

HSSP

P27251; 2DEF. [HSSP ENTRY / PDB]

ModBase

O66847.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_579-MON; -.

Ontologies

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: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

1193265; -.

AE000657_GR; aq_579.

aae:aq_579; -.

fig|224324.1.peg.422; -.

Phylogenomic databases

HOGENOM

O66847; -.

Genome annotation databases

CMR

O66847; aq_579.

Other

ProtoNet

O66847.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Hydrolase; Iron; Metal-binding; Protein biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 169`	`169`	`Peptide deformylase.`	`PRO_0000082732`
`ACT_SITE`	`136 136`		`By similarity.`
`METAL`	`93 93`		`Iron (By similarity).`
`METAL`	`135 135`		`Iron (By similarity).`
`METAL`	`139 139`		`Iron (By similarity).`

Sequence information

Length: 169 AA [This is the length of the unprocessed precursor]

Molecular weight: 19270 Da [This is the MW of the unprocessed precursor]

CRC64: 2C20014DFB199B6E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVRDIVIYPN EILKKPTEKV DVIDKEVKNL IRDMFDTMYE AEGVGLAANQ IGVPLSVMVI 

        70         80         90        100        110        120 
DTSPKEDAPP LKLVLINPEI KEGEGKIKYK EGCLSFPGLS VEVERFQKVK VNALNEHGEP 

       130        140        150        160 
VELTLEGFPA IVFQHELDHL KGITFVDRLK GWRRRMALEK YQKLLKSRK

O66847 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools