NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Reith M.E., Singh R.K., Curtis B., Boyd J., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J., Johnson S., Brown L.;
"The genome sequence of Aeromonas salmonicida subsp. salmonicida A449.";
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.

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

CP000644; ABO92079.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001143827.1; -.

3D structure databases

ModBase

A4ST57.

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.

ProtoNet

A4ST57.

Genome annotation databases

GeneID

4997273; -.

GenomeReviews

CP000644_GR; ASA_4140.

KEGG

asa:ASA_4140; -.

CMR

A4ST57; ASA_4140.

Other

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`	`1 170`	`170`	`Peptide deformylase.`	`PRO_0000300999`
`ACT_SITE`	`134 134`		`By similarity.`
`METAL`	`91 91`		`Iron (By similarity).`
`METAL`	`133 133`		`Iron (By similarity).`
`METAL`	`137 137`		`Iron (By similarity).`

Sequence information

Length: 170 AA [This is the length of the unprocessed precursor]

Molecular weight: 19432 Da [This is the MW of the unprocessed precursor]

CRC64: A324FB6DECD4B29B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAILDVLRFP DERLRTVAAP VETFTPELQH IVDDMFETMY AEEGIGLAAT QVDIHQRIIV 

        70         80         90        100        110        120 
IDVSENREDP LVLINPEILE QAGSTGIEEG CLSVPDHRAL VPRAEWVKVR ALDRNGQPFE 

       130        140        150        160        170 
LEADDLLAIC IQHEMDHLIG KLFVDYLSPL KRQRIRQKLE KMAREDRKAL

A4ST57 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