[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1093/emboj/19.21.5916; PubMed=11060042 [NCBI, ExPASy, EBI, Israel, Japan] Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.; "Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms."; EMBO J. 19:5916-5929(2000).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. Lonetto M.A., Zhu Y., Li X., Southan C.; "A human homolog of bacterial peptide deformylases."; Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Placenta; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	MITOCHONDRIAL TRANSIT PEPTIDE. DOI=10.1074/jbc.M309770200; PubMed=14532271 [NCBI, ExPASy, EBI, Israel, Japan] Serero A., Giglione C., Sardini A., Martinez-Sanz J., Meinnel T.; "An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway."; J. Biol. Chem. 278:52953-52963(2003).

Comments

FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins (By similarity).
CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H₂O = formate + methionyl peptide.
COFACTOR: Binds 1 Fe(2+) ion (By similarity).
SUBCELLULAR LOCATION: Mitochondrion (Potential).
TISSUE SPECIFICITY: Ubiquitous.
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

AF239156; AAG33968.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF322879; AAK15624.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019912; AAH19912.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_071736.1; -.

UniGene

Hs.693727

3D structure databases

HSSP

P27251; 1G2A. [HSSP ENTRY / PDB]

ModBase

Q9HBH1.

Organism-specific databases

HGNC:30012; PDF.

PDF.

Gene expression databases

ArrayExpress

Q9HBH1; -.

GermOnline

ENSG00000157312; Homo sapiens.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from HGNC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0042586;	Molecular function: peptide deformylase activity (inferred from direct assay from HGNC).
GO:0031365;	Biological process: N-terminal protein amino acid modification (inferred from direct assay from HGNC).
GO:0018206;	Biological process: peptidyl-methionine modification (inferred from direct assay from HGNC).
GO:0008284;	Biological process: positive regulation of cell proliferation (inferred from mutant phenotype from HGNC).
GO:0006412;	Biological process: translation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

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.

PRINTS

PR01576; PDEFORMYLASE.

ProDom

PD003844; Fmet_deformylase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

ProtoNet

Q9HBH1.

Proteomic databases

PeptideAtlas

Q9HBH1; -.

Genome annotation databases

Ensembl

ENSG00000157312; Homo sapiens. [Contig view]

GeneID

64146; -.

KEGG

hsa:64146; -.

NMPDR

fig|9606.3.peg.12472; -.

Phylogenomic databases

HOVERGEN

Q9HBH1; -.

Other

NextBio

66046; -.

UniRef

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

Keywords

Hydrolase; Iron; Metal-binding; Mitochondrion; Protein biosynthesis; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 39`	`39`	`Mitochondrion (Probable).`
`CHAIN`	`40 243`	`204`	`Peptide deformylase, mitochondrial.`	`PRO_0000006729`
`ACT_SITE`	`215 215`		`By similarity.`
`METAL`	`172 172`		`Iron (By similarity).`
`METAL`	`214 214`		`Iron (By similarity).`
`METAL`	`218 218`		`Iron (By similarity).`
`CONFLICT`	`11 11`		`W -> R (in Ref. 3; AAH19912).`

Sequence information

Length: 243 AA [This is the length of the unprocessed precursor]

Molecular weight: 27013 Da [This is the MW of the unprocessed precursor]

CRC64: B15A3456F0F8D689 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MARLWGALSL WPLWAAVPWG GAAAVGVRAC SSTAAPDGVE GPALRRSYWR HLRRLVLGPP 

        70         80         90        100        110        120 
EPPFSHVCQV GDPVLRGVAA PVERAQLGGP ELQRLTQRLV QVMRRRRCVG LSAPQLGVPR 

       130        140        150        160        170        180 
QVLALELPEA LCRECPPRQR ALRQMEPFPL RVFVNPSLRV LDSRLVTFPE GCESVAGFLA 

       190        200        210        220        230        240 
CVPRFQAVQI SGLDPNGEQV VWQASGWAAR IIQHEMDHLQ GCLFIDKMDS RTFTNVYWMK 


VND

Q9HBH1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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