GCW_03600







Uniprot: A0A0F6CLC4
Description: peptide deformylase
EC number: 3.5.1.88
Annotation score: 2 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide. {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS00314723}.
Cofactor: COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-Rule:MF_00163}; ; Note=Binds 1 Fe(2+) ion. {ECO:0000256|HAMAP-Rule:MF_00163}
Enzyme regulation: 
Function [CC]: 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. {ECO:0000256|HAMAP-Rule:MF_00163}.
Pathway: 
Active site: ACT_SITE 159 159 {ECO:0000256|HAMAP-Rule:MF_00163}.
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: METAL 114 114 Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.; METAL 158 158 Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.; METAL 162 162 Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
Nucleotide binding: 
Site: 
Gene names (primary): def
Gene names (synonym): 
Mass: 22,869
Subunit structure [CC]: 
Gene ontology (GO): iron ion binding [GO:0005506]; peptide deformylase activity [GO:0042586]; translation [GO:0006412]
Gene ontology IDs: GO:0005506; GO:0006412; GO:0042586
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the polypeptide deformylase family. {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS00539564}.
Protein families: Polypeptide deformylase family
Coiled coil: 
Domain [FT]: 
Motif: 
Region: 
EMBL: CP006916
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: AHB99896
UniPathway: K01462
CDD: 
Gene3D: cd00487
HAMAP: 3.90.45.10
InterPro: MF_00163
PANTHER: IPR023635
PIRSF: PTHR10458
PRINTS: PIRSF004749
PROSITE: PR01576
Pfam: 
ProDom: PF01327
SMART: 
SUPFAM: 
TIGRFAMs: SSF56420
860576-861167(+)

>nucleotide sequence
ATGAAAAGTAAATTAAAACCCACTAATGACTGATTAGTAACTGATGATAATCCCAAGATG
CGTGAAGTATGTACTGAGGTAAAATTCCCCTTAAGTCAAGAAGTGCTAGATATCATCGAT
AAGATGTTAGCTTATGTAGATGAAAGCTTTGATGACAATGCCGAAAAGTATGATATCCGT
CCAGGGATTGGGATAGCTGCTAACCAATTAGGTTTAAATCAAAGATTTTTTTATGTTCAT
TTTACTGATTTTTGTCAAAAAGAACATCGATACTTACTGATCAATCCTGAATGGATTGAT
AAGAGTCTTAACAAAGCTTACTTAGCTGTTGGTGAGGGTTGTTTATCAGTTCCCAAAGAT
AAAGATGGTTATGTAATTCGAAGTGAAACCGTTAAACTTAAAGGGTTCGATTACTTAACA
CAAAAAGATGTTGAGATCAGTGCCCATGGATTATTAGCCATGTGCTTACAACATGAGATG
GATCATTTAGAAGGTAAGTTTTATTATGATTCAATCAACATGATGAAACCATACTTTAAA
AAAGATGAGTGAGTTAGCATTGATCAAAAAGTGTGTGATCAATGTAAATAA


>protein sequence
MKSKLKPTNDWLVTDDNPKMREVCTEVKFPLSQEVLDIIDKMLAYVDESFDDNAEKYDIR
PGIGIAANQLGLNQRFFYVHFTDFCQKEHRYLLINPEWIDKSLNKAYLAVGEGCLSVPKD
KDGYVIRSETVKLKGFDYLTQKDVEISAHGLLAMCLQHEMDHLEGKFYYDSINMMKPYFK
KDEWVSIDQKVCDQCK






















© Fisunov Lab of Proteomics, 2016.