Reviewed, UniProtKB/Swiss-Prot Q9FV54 (DEF1B_SOLLC)

Names and origin

Protein names

Recommended name:
    Peptide deformylase 1B, chloroplastic
      Short name=PDF 1B
    EC=3.5.1.88
Alternative name(s):
    Polypeptide deformylase

Gene names

Name:

PDF1B

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (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 Fe2+ ion By similarity.
Subcellular location	Plastid › chloroplast Potential.
Sequence similarities	Belongs to the polypeptide deformylase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Iron Metal-binding
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptide deformylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Chloroplast Potential
	Chain	? – 279		Peptide deformylase 1B, chloroplastic		PRO_0000006733
Sites
	Active site	220	1	By similarity
	Metal binding	177	1	Iron By similarity
	Metal binding	219	1	Iron By similarity
	Metal binding	223	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9FV54-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 750F6406FDAC4233	FASTA	279	31,197
	10 20 30 40 50 60 MAMAAASWAS SSSFTRFLRP LLSRNSSPSP ISYSLHRYKS ANCLFFSASS NKPPKLAVYA 70 80 90 100 110 120 QARRVLSSKT KGDEIATPAD LSFVVPLKIV EYPDPILRAK NKRIDNFDAN LKKLVDEMFD 130 140 150 160 170 180 IMYKTDGIGL SAPQVGMNVQ LMVFNAAGER GEGEEIVLVN PRVSRYSRRI IPYEEGCLSF 190 200 210 220 230 240 PMIHGDVKRP ESVKVDAQDI NGTRFEISLS ALPARVFQHE FDHLQGVLFF DKMTDEVLDT 250 260 270 IREKLVALEK KYEDRTGLPT PESINTRKIK KAAVGFGKS

References

[1]	"Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms." Giglione C., Serero A., Pierre M., Boisson B., Meinnel T. EMBO J. 19:5916-5929(2000) [PubMed: 11060042] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF250958 mRNA. Translation: AAG33972.1.
UniGene	Les.3729
3D structure databases
SMR	Q9FV54. Positions 80-262.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.5.1.88. 281054.
Family and domain databases
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]
PRINTS	PR01576. PDEFORMYLASE.
TIGRFAMs	TIGR00079. pept_deformyl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DEF1B_SOLLC

Accession

Primary (citable) accession number: Q9FV54

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	March 1, 2001
Last modified:	February 9, 2010
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)